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PMID: 4515630 Published · ppublish English Journal Article

Proposed molecular mechanism for the action of molybedenum in enzymes: coupled proton and electron transfer.

Stiefel EI

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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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1973-04-00
Pages
988-92
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433408
Subset
IM
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