Mo(V) Electron Paramagnetic Resonance Signals from the Periplasmic Nitrate Reductase of Thiosphaera Pantotropha
Abstract
A Mo(V) electron paramagnetic resonance (EPR) study of the periplasmic respiratory nitrate reductase of the denitrifying bacterium Thiosphaera pantotropha has revealed that the molybdenum centre of this enzyme is very similar to that in the assimilatory nitrate reductase of Azotobacter vinelandii but is somewhat different from that of the membrane‐bound bacterial respiratory nitrate reductases such as those of Escherichia coli and Paracoccus denitrifcans. We have identified the Mo(V) species most likely to be the catalytically relevant one and characterised two other sets of Mo(V) EPR signals. As well as exhibiting EPR signals with g values typical of bacterial molybdenum‐containing reductases, molybdenum‐hydroxylase‐like EPR signals can be elicited in the nitrate reductase of T. pantotropha upon treatment with excess dithionite. The only other enzyme known to display this phenomenon is the periplasmic dimethylsulphoxide reductase of Rhodobacter capsulatus. A mechanism for the generation of these signals is proposed which invokes reduction of the pterin ring of the molybdenum cofactor linked to GMP from the dihydro to the tetrahydro state. The possibilities and implications of there being cysteine ligands to the molybdenum centres of these two enzymes are discussed.
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Removal of NapB from the NapAB complex reduces the efficiency of the monomer only 4-6 fold in R. sphaeroides but 30 fold in Thiosphaera pantotropha.
“Removal of NapB from the NapAB complex reduces the efficiency of the monomer only 4–6 fold in R. sphaeroides186 but 30 fold in Thiosphaera pantotropha.214”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [214]
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- Authors
- Bennett, B., Berks, B. C., Ferguson, S. J., Thomson, A. J., & Richardson, D. J.
- Affiliations
- University of East Anglia (GB)
- University of Oxford (GB)
- Corresponding author
- Bennett, Brian
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1994-12
- Volume
- 226
- Issue
- 3
- Pages
- 789-798
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2053732028
- Cited by
- 58
- References
- 0
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2018: 1 · 2017: 1 · 2014: 2 · 2013: 3 · 2012: 1
- FWCI
- 5.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- e-Publications@Marquette (Marquette University) (submittedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion)
- Funders
- Wellcome Trust
- 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, Thiosphaera pantotropha, molybdenum cofactor, sodium dithionite, good manufacturing practices, cysteine ligands, denitrifying bacteria, Rhodobacter capsulatus, enzyme mechanism
- MeSH terms
- Azotobacter, Chromatiaceae, Dithionite, Electron Spin Resonance Spectroscopy, Escherichia coli, Molybdenum, Nitrate Reductases, Paracoccus denitrificans, Rhodobacter capsulatus, Nitrate Reductase
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