Biomimetic oxidation and asymmetric reduction with coenzyme NAD analogs

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6 Citations (Scopus)

Abstract

Coenzyme NAD+/NADH, a major cofactor of dehydrogenases, functions as an autorecycling redox agent in biological systems, which is exemplified by enantioselective reduction of pyruvate to L-lactate and oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as is observed in anaerobic glycolysis. This article reviews biomimetic asymmetric reduction and oxidation in NAD+/NADH model systems. The first part outlines highly enantioselective reduction of benzoylformate, a lactate analog, with representative NADH model compounds mimicking biological reduction in lactate dehydrogenase. In this section, the well-developed model reactions are grouped based on the types of NADH models; one having a chiral center at the C-4 position of its 1,4-dihydronicotinoyl ring and the other good for recycling use. The latter half describes the detailed history on the less developed biomimetic oxidation with NAD+ model compounds. This section classifies the model reactions based on the types of model substrates to summarize the oxidation of alcohols, aldehydes, and formates into aldehydes (or ketones), carboxylates, and carbon dioxide, respectively, with regioselective formation of the corresponding NADH model compounds as analogous reactions in alcohol-, glyceraldehyde-3-phosphate-, and formate dehydrogenases.

Original languageEnglish
Pages (from-to)512-522
Number of pages11
JournalYuki Gosei Kagaku Kyokaishi/Journal of Synthetic Organic Chemistry
Volume57
Issue number6
Publication statusPublished - 1999
Externally publishedYes

Fingerprint

Coenzymes
Biomimetics
NAD
Oxidation
Aldehydes
Lactic Acid
Formates
Formate Dehydrogenases
Glyceraldehyde 3-Phosphate
Alcohols
Glyceraldehyde-3-Phosphate Dehydrogenases
Biological systems
Ketones
Pyruvic Acid
L-Lactate Dehydrogenase
Carbon Dioxide
Recycling
Oxidoreductases
Substrates

Keywords

  • 1,4-Dihydropyridines
  • Biological redox reactions
  • Biomimetic oxidation and asymmetric reduction
  • Coenzyme NAD/NADH models
  • Dehydrogenases
  • Enantioselectivity
  • Pyridinium salts
  • Regiospecificity

ASJC Scopus subject areas

  • Organic Chemistry

Cite this

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title = "Biomimetic oxidation and asymmetric reduction with coenzyme NAD analogs",
abstract = "Coenzyme NAD+/NADH, a major cofactor of dehydrogenases, functions as an autorecycling redox agent in biological systems, which is exemplified by enantioselective reduction of pyruvate to L-lactate and oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as is observed in anaerobic glycolysis. This article reviews biomimetic asymmetric reduction and oxidation in NAD+/NADH model systems. The first part outlines highly enantioselective reduction of benzoylformate, a lactate analog, with representative NADH model compounds mimicking biological reduction in lactate dehydrogenase. In this section, the well-developed model reactions are grouped based on the types of NADH models; one having a chiral center at the C-4 position of its 1,4-dihydronicotinoyl ring and the other good for recycling use. The latter half describes the detailed history on the less developed biomimetic oxidation with NAD+ model compounds. This section classifies the model reactions based on the types of model substrates to summarize the oxidation of alcohols, aldehydes, and formates into aldehydes (or ketones), carboxylates, and carbon dioxide, respectively, with regioselective formation of the corresponding NADH model compounds as analogous reactions in alcohol-, glyceraldehyde-3-phosphate-, and formate dehydrogenases.",
keywords = "1,4-Dihydropyridines, Biological redox reactions, Biomimetic oxidation and asymmetric reduction, Coenzyme NAD/NADH models, Dehydrogenases, Enantioselectivity, Pyridinium salts, Regiospecificity",
author = "Nobuhiro Kanomata",
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volume = "57",
pages = "512--522",
journal = "Yuki Gosei Kagaku Kyokaishi/Journal of Synthetic Organic Chemistry",
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T1 - Biomimetic oxidation and asymmetric reduction with coenzyme NAD analogs

AU - Kanomata, Nobuhiro

PY - 1999

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N2 - Coenzyme NAD+/NADH, a major cofactor of dehydrogenases, functions as an autorecycling redox agent in biological systems, which is exemplified by enantioselective reduction of pyruvate to L-lactate and oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as is observed in anaerobic glycolysis. This article reviews biomimetic asymmetric reduction and oxidation in NAD+/NADH model systems. The first part outlines highly enantioselective reduction of benzoylformate, a lactate analog, with representative NADH model compounds mimicking biological reduction in lactate dehydrogenase. In this section, the well-developed model reactions are grouped based on the types of NADH models; one having a chiral center at the C-4 position of its 1,4-dihydronicotinoyl ring and the other good for recycling use. The latter half describes the detailed history on the less developed biomimetic oxidation with NAD+ model compounds. This section classifies the model reactions based on the types of model substrates to summarize the oxidation of alcohols, aldehydes, and formates into aldehydes (or ketones), carboxylates, and carbon dioxide, respectively, with regioselective formation of the corresponding NADH model compounds as analogous reactions in alcohol-, glyceraldehyde-3-phosphate-, and formate dehydrogenases.

AB - Coenzyme NAD+/NADH, a major cofactor of dehydrogenases, functions as an autorecycling redox agent in biological systems, which is exemplified by enantioselective reduction of pyruvate to L-lactate and oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as is observed in anaerobic glycolysis. This article reviews biomimetic asymmetric reduction and oxidation in NAD+/NADH model systems. The first part outlines highly enantioselective reduction of benzoylformate, a lactate analog, with representative NADH model compounds mimicking biological reduction in lactate dehydrogenase. In this section, the well-developed model reactions are grouped based on the types of NADH models; one having a chiral center at the C-4 position of its 1,4-dihydronicotinoyl ring and the other good for recycling use. The latter half describes the detailed history on the less developed biomimetic oxidation with NAD+ model compounds. This section classifies the model reactions based on the types of model substrates to summarize the oxidation of alcohols, aldehydes, and formates into aldehydes (or ketones), carboxylates, and carbon dioxide, respectively, with regioselective formation of the corresponding NADH model compounds as analogous reactions in alcohol-, glyceraldehyde-3-phosphate-, and formate dehydrogenases.

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