ArticleThe Journal of biological chemistry2010
Study of the individual cytochrome b5 and cytochrome b5 reductase domains of Ncb5or reveals a unique heme pocket and a possible role of the CS domain.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- Evaluation of AlphaFold3 for Predicting Human Heme-Binding Protein Structures.International journal of molecular sciences · 2026Article
- A functional map of phosphoprotein phosphatase regulation identifies an evolutionarily conserved reductase for the catalytic metal ions.Nature communications · 2026Article
- Unique electron transfer system of cytochrome P450 monooxygenase includes a mechanism of fatty acid β-oxidation.Communications biology · 2025Article
- Inflammation-induced epigenetic imprinting regulates intestinal stem cells.Cell stem cell · 2024Article
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- The Multienzyme Complex Nature of Dehydroepiandrosterone Sulfate Biosynthesis.International journal of molecular sciences · 2024Article
- A genome-wide association study for the fatty acid composition of breast meat in an F2 crossbred chicken population.Journal of animal science and technology · 2023Article
- Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Review
- Assessing Genomic Diversity and Selective Pressures in Bohai Black Cattle Using Whole-Genome Sequencing Data.Animals : an open access journal from MDPI · 2022Article
- Structural Features of CytochromeInternational journal of molecular sciences · 2021Review
- Assessing genomic diversity and signatures of selection in Jiaxian Red cattle using whole-genome sequencing data.BMC genomics · 2021Review
- Electron Paramagnetic Resonance Spectroscopy as a Probe of Hydrogen Bonding in Heme-Thiolate Proteins.Inorganic chemistry · 2019Article
- Crystal structures of the naturally fused CS and cytochrome bActa crystallographica. Section D, Structural biology · 2019Article
- Advances in the Understanding of Protein-Protein Interactions in Drug Metabolizing Enzymes through the Use of Biophysical Techniques.Frontiers in pharmacology · 2017Review
- Lipotoxicity in the liver.World journal of hepatology · 2013Review
- Ncb5or deficiency increases fatty acid catabolism and oxidative stress.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
NADH cytochrome b(5) oxidoreductase (Ncb5or) is found in animals and contains three domains similar to cytochrome b(5) (b(5)), CHORD-SGT1 (CS), and cytochrome b(5) reductase (b(5)R). Ncb5or has an important function, as suggested by the diabetes and lipoatrophy phenotypes in Ncb5or null mice. To elucidate the structural and functional properties of human Ncb5or, we generated its individual b(5) and b(5)R domains (Ncb5or-b(5) and Ncb5or-b(5)R, respectively) and compared them with human microsomal b(5) (Cyb5A) and b(5)R (Cyb5R3). A 1.25 Å x-ray crystal structure of Ncb5or-b(5) reveals nearly orthogonal planes of the imidazolyl rings of heme-ligating residues His(89) and His(112), consistent with a highly anisotropic low spin EPR spectrum. Ncb5or is the first member of the cytochrome b(5) family shown to have such a heme environment. Like other b(5) family members, Ncb5or-b(5) has two helix-loop-helix motifs surrounding heme. However, Ncb5or-b(5) differs from Cyb5A with respect to location of the second heme ligand (His(112)) and of polypeptide conformation in its vicinity. Electron transfer from Ncb5or-b(5)R to Ncb5or-b(5) is much less efficient than from Cyb5R3 to Cyb5A, possibly as a consequence of weaker electrostatic interactions. The CS linkage probably obviates the need for strong interactions between b(5) and b(5)R domains in Ncb5or. Studies with a construct combining the Ncb5or CS and b(5)R domains suggest that the CS domain facilitates docking of the b(5) and b(5)R domains. Trp(114) is an invariant surface residue in all known Ncb5or orthologs but appears not to contribute to electron transfer from the b(5)R domain to the b(5) domain.
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