Molybdenum cofactors, enzymes and pathways

Schwarz, Günter; Mendel, Ralf R.; Ribbe, Markus W.

doi:10.1038/nature08302

Cited by 872Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsPorphyrin Metabolism and Disorders

Molybdenum cofactors, enzymes and pathways

Schwarz, Günter, Mendel, Ralf R., Ribbe, Markus W.·2009·Nature

DOI 10.1038/nature08302

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Abstract

The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. Nature has developed two scaffolds holding molybdenum in place, the iron-molybdenum cofactor and pterin-based molybdenum cofactors. Despite the different structures and functions of molybdenum-dependent enzymes, there are important similarities, which we highlight here. The biosynthetic pathways leading to both types of cofactor have common mechanistic aspects relating to scaffold formation, metal activation and cofactor insertion into apoenzymes, and have served as an evolutionary 'toolbox' to mediate additional cellular functions in eukaryotic metabolism.

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Authors: Schwarz, G., Mendel, R. R., & Ribbe, M. W.
Affiliations: University of Cologne (DE)
Technische Universität Braunschweig (DE)
University of California, Irvine (US)
ORCID: Schwarz, Günter
Ribbe, Markus W.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2009-08-12
Volume: 460
Issue: 7257
Pages: 839-847
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature08302
OpenAlex: W2088150699
Cited by: 872
References: 104
Citations by year: 2026: 44 · 2025: 67 · 2024: 65 · 2023: 51 · 2022: 49 · 2021: 55 · 2020: 43 · 2019: 61 · 2018: 46 · 2017: 58 · 2016: 42 · 2015: 47 · 2014: 56 · 2013: 44 · 2012: 52
FWCI: 2.37
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft
National Institute of General Medical Sciences (GM67626, R01GM067626)
Topics: Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
Keywords: molybdenum cofactor, iron-molybdenum cofactor, nitrogenase, nitrate reductase, sulphite oxidase, xanthine oxidoreductase, cofactor biosynthesis, metal activation, eukaryotic metabolism, trace elements
MeSH terms: Molybdenum Cofactors, Animals, Coenzymes, Copper, Enzymes, Humans, Iron, Metalloproteins, Nucleotides, Pteridines, Pterins

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Molybdenum cofactors, enzymes and pathways

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