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Literature summary for 1.14.13.208 extracted from

  • Liao, R.; Siegbahn, P.
    Mechanism and selectivity of the dinuclear iron benzoyl-coenzyme A epoxidase BoxB (2015), Chem. Sci., 6, 2754-2764 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a non-heme diiron enzyme. The two iron ions are bridged by a glutamate (Glu150). The first Fe2+ is ligated by a glutamate (Glu120) and a histidine (His153), while the second Fe2+ is ligated by an aspartate (Asp211), a glutamate (Glu240) and a histidine (His243) Aromatoleum evansii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
benzoyl-CoA + NADPH + H+ + O2 Aromatoleum evansii
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2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O
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additional information Aromatoleum evansii benzoyl-CoA epoxidase is a dinuclear iron enzyme that catalyzes the epoxidation reaction of the aromatic ring of benzoyl-CoA with chemo-, regio- and stereo-selectivity. The enzyme may also catalyze the deoxygenation reaction of epoxide, suggesting a unique bifunctionality among the diiron enzymes ?
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Organism

Organism UniProt Comment Textmining
Aromatoleum evansii Q9AIX7
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Reaction

Reaction Comment Organism Reaction ID
benzoyl-CoA + NADPH + H+ + O2 = 2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O epoxidation starts with the binding of the O2 molecule to the diferrous center to generate a diferric peroxide complex, followed by concerted O-O bond cleavage and epoxide formation. Two different pathways have been located, leading to (2S,3R)-epoxy and (2R,3S)-epoxy products. The barrier difference is 2.8 kcal/mol, corresponding to a diastereomeric excess of about 99:1. Further isomerization from epoxide to phenol has quite a high barrier, which cannot compete with the product release step. After product release into solution, fast epoxide-oxepin isomerization and racemization can take place easily, leading to a racemic mixture of (2S,3R) and (2R,3S) products. The deoxygenation of epoxide to regenerate benzoyl-CoA by a diferrous form of the enzyme proceeds via a stepwise mechanism. The C2-O bond cleavage happens first, coupled with one electron transfer from one iron center to the substrate, to form a radical intermediate, which is followed by the second C3-O bond cleavage. The first step is rate-limiting. Reaction mechanism, modeling and simulations, detailed overview Aromatoleum evansii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-CoA + NADPH + H+ + O2
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Aromatoleum evansii 2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O
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?
additional information benzoyl-CoA epoxidase is a dinuclear iron enzyme that catalyzes the epoxidation reaction of the aromatic ring of benzoyl-CoA with chemo-, regio- and stereo-selectivity. The enzyme may also catalyze the deoxygenation reaction of epoxide, suggesting a unique bifunctionality among the diiron enzymes Aromatoleum evansii ?
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?

Synonyms

Synonyms Comment Organism
benzoyl-CoA epoxidase
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Aromatoleum evansii
benzoyl-coenzyme A epoxidase
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Aromatoleum evansii
BoxB
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Aromatoleum evansii

Cofactor

Cofactor Comment Organism Structure
NADPH
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Aromatoleum evansii

General Information

General Information Comment Organism
additional information benzoyl-CoA substrate forms two hydrogen bonds with Gln116, which in turn is hydrogen-bonded to Glu120. A number of other second-shell residues are also important for the orientation of the benzoyl moiety, including Thr119, Ser123, Phe193, Phe203, and Thr210. Optimized structure of the BoxB active site with the truncated benzoyl-CoA and O2 substrates bound, corresponding to the Michaelis complex, enzyme structure and reaction mechanism mechanics/molecular mechanics calculations and modeling, overview Aromatoleum evansii