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.
MeSH Terms
Aldehyde Oxidoreductases/metabolism
Catalysis
Electron Transport
Enzymes/metabolism
Ligands
Models, Chemical
Molybdenum
Nitrates
Nitrogen
Oxidoreductases/metabolism
Protons
Xanthine Oxidase/metabolism
Chemicals
Enzymes
Ligands
Nitrates
Protons
Molybdenum
Oxidoreductases
Xanthine Oxidase
Aldehyde Oxidoreductases
Nitrogen
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Stiefel E I
References (23)
23 references, click to expand
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