Structural highlights
Function
NB5R3_PIG Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.[:]
Publication Abstract from PubMed
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(5) 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(5) reductase.
Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b(5) reductase.,Hirano Y, Kurihara K, Kusaka K, Ostermann A, Hikita M, Kimura S, Miki K, Tamada T Structure. 2025 Oct 30:S0969-2126(25)00393-4. doi: 10.1016/j.str.2025.10.006. PMID:41172987[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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 Oct 30:S0969-2126(25)00393-4. PMID:41172987 doi:10.1016/j.str.2025.10.006
