Cited by 45Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

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González, Pablo J., Rivas, María G., Brondino, Carlos D., Bursakov, Sergey A., Moura, Isabel, Moura, José J. G.·2006·JBIC Journal of Biological Inorganic Chemistry

Abstract

Nitrate reductases are enzymes that catalyze the conversion of nitrate to nitrite. We report here electron paramagnetic resonance (EPR) studies in the periplasmic nitrate reductase isolated from the sulfate-reducing bacteria Desulfovibrio desulfuricans ATCC 27774. This protein, belonging to the dimethyl sulfoxide reductase family of mononuclear Mo-containing enzymes, comprises a single 80-kDa subunit and contains a Mo bis(molybdopterin guanosine dinucleotide) cofactor and a [4Fe-4S] cluster. EPR-monitored redox titrations, carried out with and without nitrate in the potential range from 200 to -500 mV, and EPR studies of the enzyme, in both catalytic and inhibited conditions, reveal distinct types of Mo(V) EPR-active species, which indicates that the Mo site presents high coordination flexibility. These studies show that nitrate modulates the redox properties of the Mo active site, but not those of the [4Fe-4S] center. The possible structures and the role in catalysis of the distinct Mo(V) species detected by EPR are discussed.

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  • Studies with D. desulfuricans suggest that the 'nitrate species' is not catalytically relevant.

    “Studies with D. desulfuricans suggest that the ‘nitrate species’ is not catalytically relevant.120,246”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [246]

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Research works printed but not linked: 1

  1. Gonza´lez PJ, Correia C, Moura I, Brondino CD, Moura JJG (2006) J Inorg Biochem (in press) 2. Richardson DJ (2000) Microbiology 146:551-571

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Authors
González, P. J., Rivas, M. G., Brondino, C. D., Bursakov, S. A., Moura, I., & Moura, J. J. G.
Affiliations
  • Universidade Nova de Lisboa (PT)
  • Universidad Nacional del Litoral (AR)
Corresponding author
  • Brondino, Carlos D.
  • Moura, José J. G.
Venue
JBIC Journal of Biological Inorganic Chemistry
Published
2006-05-09
Volume
11
Issue
5
Pages
609-616
ISSN
  • 0949-8257 (ISSN-L)
  • 1432-1327
OpenAlex
W2041700342
Cited by
45
References
37
Citations by year
2026: 1 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 3 · 2014: 5 · 2013: 4 · 2012: 4
FWCI
2.83
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)
  • CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
Funders
  • Consejo Nacional de Investigaciones Científicas y Técnicas
  • Fundação para a Ciência e a Tecnologia
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
periplasmic nitrate reductase, Desulfovibrio desulfuricans, molybdenum enzymes, [4Fe-4S] cluster, redox titration, enzyme inhibition, coordination flexibility, enzyme catalysis
MeSH terms
Bacterial Proteins, Binding Sites, Catalysis, Electron Spin Resonance Spectroscopy, Guanine Nucleotides, Molybdenum, Nitrates, Oxidation-Reduction, Pterins, Periplasm, Desulfovibrio desulfuricans, Nitrate Reductase

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