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. 1973 Apr;70(4):988–992. doi: 10.1073/pnas.70.4.988

Proposed Molecular Mechanism for the Action of Molybdenum in Enzymes: Coupled Proton and Electron Transfer

Edward I Stiefel 1
PMCID: PMC433408  PMID: 4515630

Abstract

The reactions catalyzed by Mo enzymes each find the product differing from the substrate by two electrons and two protons (or some multiple thereof). The coordination chemistry of Mo suggests that there is a distinct relationship between acid-base and redox properties of Mo complexes, and that a coupled electron-proton transfer (to or from substrate) may be mediated by Mo in enzymes. Each of the Mo enzymes (nitrogenase, nitrate reductase, xanthine oxidase, aldehyde oxidase, and sulfite oxidase) is discussed; it is shown that a simple molecular mechanism embodying coupled proton-electron transfer can explain many key experimental observations. In view of this mechanism, the reasons for the use of Mo (from an evolutionary and chemical point of view) are discussed and other metals that may replace Mo are considered.

Keywords: metalloenzymes, nitrogenase, nitrate reductase, xanthine oxidase, ligand acidity

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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