ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2012
Laue crystal structure of Shewanella oneidensis cytochrome c nitrite reductase from a high-yield expression system.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed.
- Lysine or histidine? examining the role of the proximal ligand at the active heme center of cytochrome c nitrite reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Roles of Three Conserved Active Site Residues of CytochromeJournal of the American Chemical Society · 2025Article
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- Bioremediation Performance of Recombinant Shewanella azerbaijanica; Considering Uranium Removal in the Presence of Nitrate.Current microbiology · 2025Article
- Electrocatalytic Nitrite Reduction by a Monomeric NrfA: Commonality in Ammonification Mechanisms.Biochemistry · 2025Article
- Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization.IUCrJ · 2025Article
- Trichlorobacter ammonificans, a dedicated acetate-dependent ammonifier with a novel module for dissimilatory nitrate reduction to ammonia.The ISME journal · 2023Article
- Homology modeling and virtual characterization of cytochrome c nitrite reductase (NrfA) in three model bacteria responsible for short-circuit pathway, DNRA in the terrestrial nitrogen cycle.World journal of microbiology & biotechnology · 2022Article
- Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- CytochromeThe Journal of biological chemistry · 2020Article
- Time-Resolved Macromolecular Crystallography at Pulsed X-ray Sources.International journal of molecular sciences · 2019Review
- Upon further analysis, neither cytochrome cJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Article
- Synthetic and Evolutionary Construction of a Chlorate-Reducing Shewanella oneidensis MR-1.mBio · 2015Article
- Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities.Journal of the Royal Society, Interface · 2015Review
- Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1.Frontiers in microbiology · 2015Article
- Hydrogen bonding networks tune proton-coupled redox steps during the enzymatic six-electron conversion of nitrite to ammonia.Biochemistry · 2014Article
- Shewanella oneidensis cytochrome c nitrite reductase (ccNiR) does not disproportionate hydroxylamine to ammonia and nitrite, despite a strongly favorable driving force.Biochemistry · 2014Article
- A robust genetic system for producing heterodimeric native and mutant cytochrome bc(1).Biochemistry · 2013Article
- Contrasting catalytic profiles of multiheme nitrite reductases containing CxxCK heme-binding motifs.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
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Abstract
The high-yield expression and purification of Shewanella oneidensis cytochrome c nitrite reductase (ccNiR) and its characterization by a variety of methods, notably Laue crystallography, are reported. A key component of the expression system is an artificial ccNiR gene in which the N-terminal signal peptide from the highly expressed S. oneidensis protein "small tetraheme c" replaces the wild-type signal peptide. This gene, inserted into the plasmid pHSG298 and expressed in S. oneidensis TSP-1 strain, generated approximately 20 mg crude ccNiR per liter of culture, compared with 0.5-1 mg/L for untransformed cells. Purified ccNiR has nitrite and hydroxylamine reductase activities comparable to those previously reported for Escherichia coli ccNiR, and is stable for over 2 weeks in pH 7 solution at 4 °C. UV/vis spectropotentiometric titrations and protein film voltammetry identified five independent one-electron reduction processes. Global analysis of the spectropotentiometric data also allowed determination of the extinction coefficient spectra for the five reduced ccNiR species. The characteristics of the individual extinction coefficient spectra suggest that, within each reduced species, the electrons are distributed among the various hemes, rather than being localized on specific heme centers. The purified ccNiR yielded good-quality crystals, with which the 2.59-Å-resolution structure was solved at room temperature using the Laue diffraction method. The structure is similar to that of E. coli ccNiR, except in the region where the enzyme interacts with its physiological electron donor (CymA in the case of S. oneidensis ccNiR, NrfB in the case of the E. coli protein).
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