ArticleThe EMBO journal2006
X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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60 citing papers in PubMed, 166 citations in OpenAlex.
- 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
- Different grazing intensities affect soil nitrogen cycling by altering microbial nitrogen metabolism in alpine wetlands.iScience · 2026Article
- Demonstration of the Role of Both a Ttr and a Psr Homologue Enzymes in the Respiration of Tetrathionate by an Environmental Bacterium Shewanella sp. ANA-3.Environmental microbiology · 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
- Cytochrome "nanowires" are physically limited to sub-picoamp currents that suffice for cellular respiration.Frontiers in chemistry · 2025Article
- Towards understanding the crystallization of photosystem II: influence of poly(ethylene glycol) of various molecular sizes on the micelle formation of alkyl maltosides.Photosynthesis research · 2024Article
- Nitrate reduction to ammonium: a phylogenetic, physiological, and genetic aspects in Prokaryotes and eukaryotes.Archives of microbiology · 2024Review
- Characterization of the inner membrane cytochrome ImcH from Geobacter reveals its importance for extracellular electron transfer and energy conservation.Protein science : a publication of the Protein Society · 2023Article
- Article
- A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.Nature communications · 2023Article
- Cryo-EM structure of an extracellular Geobacter OmcE cytochrome filament reveals tetrahaem packing.Nature microbiology · 2022Article
- 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
- Review
- Deletion of the cytochrome bc complex from Heliobacterium modesticaldum results in viable but non-phototrophic cells.Photosynthesis research · 2021Article
- Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin.The Biochemical journal · 2021Article
- Crossing the Wall: Characterization of the Multiheme Cytochromes Involved in the Extracellular Electron Transfer Pathway ofMicroorganisms · 2021Article
- A Hybrid Extracellular Electron Transfer Pathway Enhances the Survival of Vibrio natriegens.Applied and environmental microbiology · 2020Article
- CytochromeThe Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oxidation of membrane-bound quinol molecules is a central step in the respiratory electron transport chains used by biological cells to generate ATP by oxidative phosphorylation. A novel family of cytochrome c quinol dehydrogenases that play an important role in bacterial respiratory chains was recognised in recent years. Here, we describe the first structure of a cytochrome from this family, NrfH from Desulfovibrio vulgaris, which forms a stable complex with its electron partner, the cytochrome c nitrite reductase NrfA. One NrfH molecule interacts with one NrfA dimer in an asymmetrical manner, forming a large membrane-bound complex with an overall alpha(4)beta(2) quaternary arrangement. The menaquinol-interacting NrfH haem is pentacoordinated, bound by a methionine from the CXXCHXM sequence, with an aspartate residue occupying the distal position. The NrfH haem that transfers electrons to NrfA has a lysine residue from the closest NrfA molecule as distal ligand. A likely menaquinol binding site, containing several conserved and essential residues, is identified.
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