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Literature summary for 1.12.7.2 extracted from

  • Adams, M.W.W.; Mortenson, L.E.
    The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I (1984), J. Biol. Chem., 259, 7045-7055.
    View publication on PubMed
Search for more literature for 1.12.7.2

Inhibitors

Inhibitors Comment Organism Structure
2,2'-bipyridyl 66% activity at 1 mM Clostridium pasteurianum
CO hydrogenase I is readily inhibited, hydrogenase II is irreversibly inactivated Clostridium pasteurianum
CuSO4 0% activity at 1 mM Clostridium pasteurianum
o-phenanthroline 36% activity at 1 mM Clostridium pasteurianum
O2 50% activity loss after 2 min Clostridium pasteurianum
phenylmethanesulfonyl fluoride 61% activity at 1 mM Clostridium pasteurianum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 reduced ferredoxin hydrogen evolution, hydrogenase I Clostridium pasteurianum
0.05
-
 reduced ferredoxin hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum
0.13
-
 reduced ferredoxin hydrogen evolution, hydrogenase II Clostridium pasteurianum
0.13
-
 reduced ferredoxin hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
0.18
-
 oxidized methylene blue hydrogen oxidation, hydrogenase I Clostridium pasteurianum
0.18
-
 oxidized methylene blue hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum
0.31
-
 oxidized methyl viologen hydrogen evolution, hydrogenase II Clostridium pasteurianum
0.31
-
 oxidized methyl viologen hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
0.4
-
 oxidized methylene blue hydrogen oxidation, hydrogenase II Clostridium pasteurianum
0.4
-
 oxidized methylene blue hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
5
-
 oxidized methyl viologen hydrogen oxidation, hydrogenase I Clostridium pasteurianum
5
-
 oxidized methyl viologen hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum
5.7
-
 oxidized methyl viologen hydrogen oxidation, hydrogenase II Clostridium pasteurianum
5.7
-
 oxidized methyl viologen hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
6.25
-
 oxidized methyl viologen hydrogen evolution, hydrogenase I Clostridium pasteurianum
6.25
-
 oxidized methyl viologen hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum

Metals/Ions

Metals/Ions Comment Organism Structure
Fe hydrogenase I contains 12 atoms per mol enzyme and hydrogenase II 8 atoms per mol enzyme Clostridium pasteurianum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2 + oxidized ferredoxin Clostridium pasteurianum
-
 H+ + reduced ferredoxin
-
 r
H2 + oxidized ferredoxin Clostridium pasteurianum W5
-
 H+ + reduced ferredoxin
-
 r

Organism

Organism UniProt Comment Textmining
Clostridium pasteurianum
-
-
-
Clostridium pasteurianum
-
 hydrogenase II, uptake hydrogenase
-
Clostridium pasteurianum
-
 hydrogenase I, bidirectional hydrogenase
-
Clostridium pasteurianum W5
-
-
-

Storage Stability

Storage Stability Organism
-180°C, 4 months, 100% activity Clostridium pasteurianum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H+ + reduced ferredoxin
-
 Clostridium pasteurianum H2 + oxidized ferredoxin
-
 r
H+ + reduced methyl viologen
-
 Clostridium pasteurianum H2 + oxidized methyl viologen
-
 r
H2 + electron acceptor methylene blue as electron acceptor Clostridium pasteurianum H+ + reduced electron acceptor
-
 ?
H2 + electron acceptor methyl viologen as electron acceptor Clostridium pasteurianum H+ + reduced electron acceptor
-
 ?
H2 + electron acceptor methylene blue as electron acceptor Clostridium pasteurianum W5 H+ + reduced electron acceptor
-
 ?
H2 + electron acceptor methyl viologen as electron acceptor Clostridium pasteurianum W5 H+ + reduced electron acceptor
-
 ?
H2 + oxidized ferredoxin
-
 Clostridium pasteurianum H+ + reduced ferredoxin
-
 r
H2 + oxidized ferredoxin
-
 Clostridium pasteurianum W5 H+ + reduced ferredoxin
-
 r
H2 + oxidized methyl viologen
-
 Clostridium pasteurianum H+ + reduced methyl viologen
-
 r
H2 + oxidized methyl viologen
-
 Clostridium pasteurianum W5 H+ + reduced methyl viologen
-
 r
H2 + oxidized methylene blue
-
 Clostridium pasteurianum H+ + reduced methylene blue
-
 r
H2 + oxidized methylene blue
-
 Clostridium pasteurianum W5 H+ + reduced methylene blue
-
 r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
 hydrogen evolution, hydrogenase II Clostridium pasteurianum
6.3
-
 hydrogen evolution, hydrogenase I Clostridium pasteurianum
7
-
 hydrogenase II, hydrogen oxidation, methylene blue as electron acceptor Clostridium pasteurianum
9.1
-
 hydrogen evolution, hydrogenase II Clostridium pasteurianum
9.8
-
 hydrogenase I, hydrogen oxidation Clostridium pasteurianum
10.5
-
 hydrogenase II, hydrogen oxidation, methylene blue as electron acceptor Clostridium pasteurianum