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| Hauptseite > Publications database > Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b5 reductase |
| Hauptseite > Publications database > Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b5 reductase |
| Journal Article | IMPULSE-2026-00002 |
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2026
Elsevier Science
London [u.a.]
Please use a persistent id in citations: doi:10.1016/j.str.2025.10.006
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 b5 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 b5 reductase.
Keyword(s): Health and Life (1st) ; Biology (2nd) ; Crystallography (2nd)
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