[28] Electroenzymatic and electromicrobial reduction: Preparation of chiral compounds

Thanos, Iordanis; Bader, Johann; Günther, Helmut; Neumann, Stefan; Krauss, Friedrich; Simon, Helmut

doi:10.1016/s0076-6879(87)36030-6

Cited by 41 publications

(13 citation statements)

References 15 publications

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“…Reductase activity of HVOR was determined at 37°C (Thanos et al, 1987). Dehydrogenase reaction was measured according to Schinschel and Simon (1993~).…”

Section: Enzyme Assays and Other Analytical Proceduresmentioning

confidence: 99%

“…The first three purification steps were carried out as described by Thanos et al (1987), with buffers containing 2 mM Na,S,O, instead of 4 mM. To obtain pure enzyme from unlabelled material an FPLC Mono Q column (Pharmacia HR 5/5) chromatography was substituted as the final purification step for the second gel-filtration chromatography on Sepharose CL-6B.…”

Section: Purification Of 99mo-labelled and Unlabelled (2r)-hydroxycarmentioning

confidence: 99%

“…The purification procedure described by Thanos et al (1987) leads to enzyme preparations with a specific activity of almost 1000 U/mg protein and was also used on a small scale starting with 4-15 g wet packed cells grown in the presence of ''Mo02-. For purifications starting with 150 g wet packed cells the second gel-filtration chromatography step on Sepharose CL-6B was substituted by an anion-exchange chromatography on a Mono Q column.…”

Section: Purification Of Radioactively Labelled and Unlabelled (2r)-hmentioning

confidence: 99%

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The (2R)‐hydroxycarboxylate‐viologen‐oxidoreductase from Proteus vulgaris is a molybdenum‐containing iron‐sulphur protein

Trautwein

Krauss

Lottspeich

et al. 1994

European Journal of Biochemistry

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An oxidoreductase with an extremely broad substrate specificity reducing reversibly 2‐oxocar‐boxylates at the expense of reduced artificial redox mediators to (2R)‐hydroxycarboxylates has been purified to a specific activity of up to 1800 μmol · min−1· mg−1 for the reduction of phenylpyruvate. The membrane‐bound non‐pyridine nucleotide‐dependent enzyme appears in the form of various oligomers of the 80‐kDa monomer. The isoelectric point is 5.1. Based on a molecular mass of 80 kDa the enzyme contains up to one molybdenum, four iron and four sulphur atoms. After growth on 99Mo‐labelled molybdate, enzyme and radioactivity coincided as shown by gel electrophoresis. Permanganate oxidation delivers 0.7 mol pterin‐6‐carboxylic acid. The molybdenum cofactor is a mononucleotide. The enzyme is inhibited by cyanide. The first 20 amino acids have been determined. The enzyme belongs to the rare group of molybdoenzymes which possess no further prosthetic groups than the iron‐sulphur clusters.

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“…Reductase activity of HVOR was determined at 37°C (Thanos et al, 1987). Dehydrogenase reaction was measured according to Schinschel and Simon (1993~).…”

Section: Enzyme Assays and Other Analytical Proceduresmentioning

confidence: 99%

Section: Purification Of 99mo-labelled and Unlabelled (2r)-hydroxycarmentioning

confidence: 99%

Section: Purification Of Radioactively Labelled and Unlabelled (2r)-hmentioning

confidence: 99%

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The (2R)‐hydroxycarboxylate‐viologen‐oxidoreductase from Proteus vulgaris is a molybdenum‐containing iron‐sulphur protein

Trautwein

Krauss

Lottspeich

et al. 1994

European Journal of Biochemistry

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“…When the electron transfer from the mediator to the enzyme is rate limiting immobilization, preferably of both the enzyme and the mediator, may be feasible to reduce the mass transfer resistance. Enoate reductase catalyzes the stereo-specific reduction of a great variety of enoates to acylates Thanos et al, 1987;Biihler and Simon, 1982;and Thanos and Simon, 1987). As a result it shows a very good potential as biocatalyst for the preparation of chiral acids (Thanos and Simon, 1987).…”

Section: Introductionmentioning

confidence: 99%

“…Enoate reductase catalyzes the stereo-specific reduction of a great variety of enoates to acylates Thanos et al, 1987;Biihler and Simon, 1982;and Thanos and Simon, 1987). As a result it shows a very good potential as biocatalyst for the preparation of chiral acids (Thanos and Simon, 1987). The reduction of the enzyme can be performed with artificial mediators like methyl viologen or other viologens.…”

Section: Introductionmentioning

confidence: 99%

Effect of the half wave potential and change of some viologens on the rate of conversion of crotonic acid into butyric acid by enoate reductase

et al. 1992

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SUMMARYThe rate of the bio-electrochemical conversion of crotonic acid into butyric acid by enoate reductase is dependent on the type of viologen used. This illustrates that the reaction between enzyme and mediator, rather than the reaction between enzyme and crotonic acid, is rate limiting. Thus for bio-electrochemical conversion of enoates into saturated chiral acids immobilization of enoate reductase is beneficial from a kinetic point of view. The highest rate constant (k'=7.0xl06 M~.s "1) was measured using mono-N-(aminopropyl) viol6gen.

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Reduction Reactions

1995

Enzyme Catalysis in Organic Synthesis

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[28] Electroenzymatic and electromicrobial reduction: Preparation of chiral compounds

Cited by 41 publications

References 15 publications

The (2R)‐hydroxycarboxylate‐viologen‐oxidoreductase from Proteus vulgaris is a molybdenum‐containing iron‐sulphur protein

The (2R)‐hydroxycarboxylate‐viologen‐oxidoreductase from Proteus vulgaris is a molybdenum‐containing iron‐sulphur protein

Effect of the half wave potential and change of some viologens on the rate of conversion of crotonic acid into butyric acid by enoate reductase

Reduction Reactions

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