Cited by 141Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

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Moura, Jos� J. G., Brondino, Carlos D., Trinc�o, Jos�, Rom�o, Maria Jo�o·2004·JBIC Journal of Biological Inorganic Chemistry

Abstract

Molybdenum and tungsten are second- and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site.

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  • The extra residues in molybdopterin proteins that share high sequence similarity are distributed over the molecular surface.

    “the extra residues are distributed over themolecular surface.187”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [187]

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Authors
Moura, J. J. G., Brondino, C. D., Trinc�o, J., & Rom�o, M. J.
Affiliations
  • Universidad Nacional del Litoral (AR)
  • Universidade Nova de Lisboa (PT)
Venue
JBIC Journal of Biological Inorganic Chemistry
Published
2004-08-12
Volume
9
Issue
7
Pages
791-799
ISSN
  • 0949-8257 (ISSN-L)
  • 1432-1327
OpenAlex
W2042816956
Cited by
141
References
54
Citations by year
2026: 3 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 6 · 2017: 7 · 2016: 4 · 2015: 4 · 2014: 9 · 2013: 6 · 2012: 12
FWCI
1.31
Type
journal article
Language
en
Open access
Locations
  • JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
molybdenum enzymes, tungsten enzymes, nitrate reductase, formate dehydrogenase, sulfite oxidase, xanthine oxidase, oxygen atom transfer, enzyme active site, metalloenzyme catalysis
MeSH terms
Electron Transport, Formate Dehydrogenases, Molybdenum, Nitrate Reductases, Tungsten, Nitrate Reductase

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