9V6A
X-ray crystal structure of the T66V mutant b5R co-crystallized with NADH
Summary for 9V6A
| Entry DOI | 10.2210/pdb9v6a/pdb |
| Descriptor | NADH-cytochrome b5 reductase 3, FLAVIN-ADENINE DINUCLEOTIDE, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | fatty acid synthesis, methemoglobin reduction, xenobiotic oxidation, antioxidant defense, oxidoreductase |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 32321.71 |
| Authors | Hirano, Y.,Kurihara, K.,Kusaka, K.,Ostermann, A.,Hikita, M.,Kimura, S.,Miki, K.,Tamada, T. (deposition date: 2025-05-27, release date: 2025-11-19) |
| Primary citation | Hirano, Y.,Kurihara, K.,Kusaka, K.,Ostermann, A.,Hikita, M.,Kimura, S.,Miki, K.,Tamada, T. Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b 5 reductase. Structure, 2025 Cited by PubMed Abstract: Many structural studies have been reported for ferredoxin:NADP reductase family members, but an experimental validation of the catalytic hydride and proton transfer steps through a direct detection of the involved hydrogen atoms has not been achieved so far. Here, we determined high-resolution X-ray and neutron crystal structures of NADH-cytochrome b reductase, which acts as an electron supplier for various metabolic processes and mediates hydride and proton transfer reactions via its FAD and NADH cofactors. The X-ray structures identify the FADH-NAD and FAD-NADH complexes based on the electron densities of the hydrogen atoms bound to the cofactors. The neutron structures determined at different pD-values show a difference in the protonation state of the histidine residue in the hydrogen-bond network from FAD to the protein surface. The observation of the hydrogen atoms reveals the structural basis for the hydride and proton transfer reactions catalyzed by NADH-cytochrome b reductase. PubMed: 41172987DOI: 10.1016/j.str.2025.10.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.94 Å) |
Structure validation
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