Cited by 40Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsElectron Spin Resonance Studies

DFT Investigation of the Molybdenum Cofactor in Periplasmic Nitrate Reductases: Structure of the Mo(V) EPR-Active Species

Biaso, Frédéric, Burlat, Bénédicte, Guigliarelli, Bruno·2012·Inorganic Chemistry

Abstract

The periplasmic nitrate reductase NAP belongs to the DMSO reductase family that regroups molybdoenzymes housing a bis-molybdopterin cofactor as the active site. Several forms of the Mo(V) state, an intermediate redox state in the catalytic cycle of the enzyme, have been evidenced by EPR spectroscopy under various conditions, but their structure and catalytic relevance are not fully understood. On the basis of structural data available from the literature, we built several models that reproduce the first coordination sphere of the molybdenum cofactor and used DFT methods to make magneto-structural correlations on EPR-detected species. "High-g" states, which are the most abundant Mo(V) species, are characterized by a low-anisotropy g tensor and a high g(min) value. We assign this signature to a six-sulfur coordination sphere in a pseudotrigonal prismatic geometry with a partial disulfide bond. The "very high-g" species is well described with a sulfido ion as the sixth ligand. The "low-g" signal can be successfully associated to a Mo(V) sulfite-oxidase-type active site with only one pterin moiety coordinated to the molybdenum ion with an oxo or sulfido axial ligand. For all these species we investigate their catalytic activity using a thermodynamic point of view on the molybdenum coordination sphere. Beyond the periplasmic nitrate reductase case, this work provides useful magneto-structural correlations to characterize EPR-detected species in mononuclear molybdoenzymes.

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Crossref · 10.1021/ic201533p

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  • A recent theoretical (QM/MM) study provided a structural rationale for the different species detected for NapA.

    “A recent theoretical (QM/MM) study provided a structural rationale for the different species detected for NapA (Fig. 13).248”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [248]

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Authors
Biaso, F., Burlat, B., & Guigliarelli, B.
Affiliations
Centre National de la Recherche Scientifique (FR)
Corresponding author
Biaso, Frédéric
Venue
Inorganic Chemistry
Published
2012-03-07
Volume
51
Issue
6
Pages
3409-3419
ISSN
  • 0020-1669 (ISSN-L)
  • 1520-510X
OpenAlex
W2321782915
Cited by
40
References
96
Citations by year
2024: 2 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 4 · 2014: 4 · 2013: 6
FWCI
1.72
Type
journal article
Language
en
Open access
closed
Locations
  • Inorganic Chemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
Centre National de la Recherche Scientifique
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 › Biophysics › Electron Spin Resonance Studies
Keywords
periplasmic nitrate reductase, molybdenum cofactor, molybdoenzymes, electron spin resonance, magneto-structural correlations, sulfido ligands, disulfide bonds, catalytic mechanism, thermodynamic analysis
MeSH terms
Molybdenum Cofactors, Coenzymes, Electron Spin Resonance Spectroscopy, Metalloproteins, Models, Molecular, Nitrate Reductases, Oxidation-Reduction, Pteridines, Periplasm

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