EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774
Open accessAbstract
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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- 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.
- ORCID
- 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
- green
- hdl.handle.net
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- 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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