ArticleThe Biochemical journal2005
Site-directed modifications indicate differences in axial haem c iron ligation between the related NrfH and NapC families of multihaem c-type cytochromes.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 35 citations in OpenAlex.
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- 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
- Deep-Sea Bacterium Shewanella piezotolerans WP3 Has Two Dimethyl Sulfoxide Reductases in Distinct Subcellular Locations.Applied and environmental microbiology · 2017Article
- Nitrate and periplasmic nitrate reductases.Chemical Society reviews · 2014Review
- Physiological and evolutionary studies of NAP systems in Shewanella piezotolerans WP3.The ISME journal · 2011Article
- Substrate specificity of three cytochrome c haem lyase isoenzymes from Wolinella succinogenes: unconventional haem c binding motifs are not sufficient for haem c attachment by NrfI and CcsA1.Molecular microbiology · 2010Article
- Membrane tetraheme cytochrome c(m552) of the ammonia-oxidizing nitrosomonas europaea: a ubiquinone reductase.Biochemistry · 2008Article
- The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species.Journal of bacteriology · 2007Article
- X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination.The EMBO journal · 2006Article
- Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
During the last decade, a number of related bacterial membrane-bound multihaem c-type cytochromes, collectively referred to as the NapC/NirT family, were identified. These proteins are generally thought to catalyse electron transport between the quinone/quinol pool and periplasmic oxidoreductases. The best-characterized members, the tetrahaem c-type cytochromes NrfH and NapC, mediate electron transport to NrfA and NapA respectively. Amino acid sequence alignments suggest that the nature and position of distal haem c iron ligands differs in NrfH and NapC proteins. Site-directed modification of potential haem c iron-ligating histidine, lysine and methionine residues in Wolinella succinogenes NrfH was performed to determine the implication in electron transport from formate to nitrite. Two histidine, one lysine and one methionine residues were found to be essential, whereas the replacement of three other conserved histidine residues, one methionine and two lysines did not prevent growth by nitrite respiration. The results contrast those previously obtained for Paracoccus pantotrophus NapC, in which four essential histidine residues have been identified that are highly likely to serve as distal haem c iron ligands. The combined experimental evidence suggests different haem ligation patterns within NapC and NrfH proteins, which might reflect their different functions in the bacterial electron transfer.
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