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Ligand heme b
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Basic Ligand Information
Fe-protoporphyrin complex, Fe-protoporphyrin IX, Fe2+-protoporphyrin, ferriprotoporphorin IX, ferriprotoporphyrin IX, ferroheme b, ferroprotoporphyrin IX, Haemin, heme, heme b556, heme b562, heme[side 1], heme[side 2], hemin, protoheme, protoheme IX
BRENDA
KEGG
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Show all BRENDA pathways known for heme b
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (76 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
672566, 681311, 684502, 685997, 690140, 688061, 688506, 685973, 688701, 690161, 688105, 686898, 688832, 687147, 686118, 687662, 687677, 688671, 686882, 684932, 687109, 689226, 688156, 688160, 686555, 689219, 684386, 688237, 688500, 686565, 687555, 686078, 690138, 685099, 687570, 685815, 688881, 688158, 684777, 689096, 686599, 684348, 686723, 684789, 690143, 685906, 685498, 688672, 684920, 686073
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
hemin + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ = biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+ = biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
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protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ = biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ = biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
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protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
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protoheme + reduced acceptor + O2 = biliverdin-IX-beta + CO + Fe2+ + acceptor + H2O
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protoheme + reduced acceptor + O2 = biliverdin-IX-delta + CO + Fe2+ + acceptor + H2O
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2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
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(2E,6E)-farnesyl diphosphate + protoheme IX + H2O = diphosphate + ferroheme o
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protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate
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In Vivo Product in Enzyme-catalyzed Reactions (15 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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Fe-coproporphyrin III + S-adenosyl-L-methionine = protoheme + CO2 + 5'-deoxyadenosine + L-methionine
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Substrate in Enzyme-catalyzed Reactions (168 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 2 NADPH + 2 H+ + 2 O2 = biliverdin + Fe2+ + CO + 2 NADP+ + H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 AH2 + 3 O2 = biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + 3 reduced ascorbate + 3 O2 = biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + AH2 + O2 = biliverdin + Fe2+ + CO + A + H2O
686723, 687570, 689226, 687677, 672566, 688671, 681311, 684386, 684502, 684777, 684789, 684932, 685815, 685906, 685997, 686118, 686555, 686599, 686898, 687555, 688105, 688237, 688832, 689096, 690140, 684920, 685498, 686078, 687109, 687147, 688061, 688158, 688160, 688506, 688881, 689219, 690138, 690143, 685973, 686073, 686565, 686882, 688156, 688672, 688701, 690161, 684348, 688500, 687662, 685099
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized electron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + electron donor + O2 = biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + NADPH + H+ + O2 = biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
hemin + reduced acceptor + O2 = alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + reduced acceptor + O2 + Fe2+ = biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced cytochrome P450 reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 = biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2 = biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
hemin + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ = biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+ = biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
-
protoheme + reduced ferredoxin [iron-sulfur] cluster + H2O2 + H+ = verdoheme + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ = biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ = biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
protoheme + 5 reduced acceptor + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
protoheme + 5 reduced acceptor + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
heme + electron donor + O2 = alpha-biliverdin + beta-biliverdin + delta-biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
heme + electron donor + O2 = biliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O
-
protoheme + reduced acceptor + O2 = biliverdin-IX-beta + CO + Fe2+ + acceptor + H2O
-
protoheme + reduced acceptor + O2 = biliverdin-IX-delta + CO + Fe2+ + acceptor + H2O
-
2 S-adenosyl-L-methionine + heme + 2 reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O = diphosphate + ferroheme o
-
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate
-
Apocytochrome c + heme = Holocytochrome c
691983, 94055, 94056, 94059, 651850, 651895, 652487, 691507, 729727, 729740, 94060, 651429, 729264, 730058, 730827, 747125, 653258, 730322, 94057, 94058, 652352, 715034
-
apocytochrome c1 + heme = holocytochrome c1
-
Product in Enzyme-catalyzed Reactions (24 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
-
Fe-coproporphyrin III + S-adenosyl-L-methionine = protoheme + CO2 + 5'-deoxyadenosine + L-methionine
-
protoporphyrin + Fe2+ = protoheme + 2 H+
34938, 34964, 34962, 34967, 34963, 34966, 34960, 34961, 34968, 34969, 34971, 34949, 34965, 34970, 34972, 0, 34933, 34935, 34939, 34942, 34943, 34945, 34946, 34973, 34936, 34947, 34948, 34932, 34934, 34937, 34944, 34941, 34974, 34930, 34931, 34940, 653206, 34959
-
ATP + H2O + heme-[dipeptide-binding protein DppA][side 1] = ADP + phosphate + heme[side 2] + [dipeptide-binding protein DppA][side 1]
-
ATP + H2O + heme-[L-alanyl-gamma-D-glutamyl-meso-diaminopimelate periplasmic binding protein MppA][side 1] = ADP + phosphate + heme[side 2] + [L-alanyl-gamma-D-glutamyl-meso-diaminopimelate periplasmic binding protein MppA][side 1]
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Enzyme Cofactor/Cosubstrate (18341 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
-
the quinohaemoprotein alcohol dehydrogenase contains heme C in both subunits, the ADH complex of contains 18 nmol of heme C per mg of protein (ratio of 3.6 mol of heme C per mol of enzyme)
-
binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer
-
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein
-
in the crystals, the four hemes in the unit cell have only two different orientations, related by an 180° rotation about the b axis. The heme rings are oriented parallel to the b axis
-
-
flavocytochrome. Binding of cellobiose to the active site inhibits electron transfer from flavin to heme
protein displays absorption maximum at 419 nm with a broad tail from about 450-480 nm, corresponding to the ferric heme and flavin groups respectively
the enzyme contains a protease-sensitive linker region, can be cleaved by endogenous proteases into a catalytically active flavin fragment and an inactive haem domain
-
cleavage of heme containing fragment by papain or V8 proteinase can convert CBO to cellobiose:quinone dehydrogenase, cytochrome b-type heme group used for storage and delivery of electrons from a two-electron donor, e.g. cellobiose, via FADH2 to one-electron acceptors, e.g. radicals, cytochrome c, ferricyanide and oxygen
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme component serves for the storage of electrons to be incorporated into molecular oxygen for direct reduction to water
heme domain increases the rate of electron transfer to one-electron acceptors
heme group: cytochrome b type, inactivated at higher pH levels, caused by conformational changes of protein, heme is necessary for reduction of cytochrome c, it acts as a single electron reductant, 35 kDa heme-containing domain
the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme
heme/iron-sulfur protein. The heme groups of the enzyme are rapidly reduced by reduced 2,3-dimethyl-1,4-naphthoquinone, which indicates that the enzyme functions as a menaquinol-acceptor oxidoreductase
-
the enzyme contains reduced hemes b and of oxygenated and ferric heme d, differing from cytochrome bd. Heme d serves as the ligand-binding site of CIO
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
-
439855, 765656, 765773, 696216, 439858, 711139, 439860, 439856, 439862, 439872, 439868, 764383, 764780, 764255, 439871, 439865, 697682, 698047, 764388, 713299, 764871, 765501, 439876, 765160, 765572, 696257, 699802, 713234, 439880, 743696, 439874, 764787, 725934, 765632, 763910, 765596, 765620, 764826, 764715, 765273
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
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enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme protein
heme protein
heme protein
heme protein
heme protein
heme protein
heme protein
heme protein
heme protein
heme protein
heme protein