Download MendeleyRedox-dependent hydrogen-bond network rearrangement of ferredoxin-NADP + reductase revealed by high-resolution X-ray and neutron crystallography.
Uenaka, M., Ohnishi, Y., Ise, A., Yu, J., Yano, N., Kusaka, K., Tanaka, H., Kurisu, G.(2025) Acta Crystallogr F Struct Biol Commun 81: 73-84
- PubMed: 39913263
- DOI: https://doi.org/10.1107/S2053230X25000524
- Primary Citation of Related Structures:
9KK7, 9KKC, 9KKG, 9KKH, 9L8G - PubMed Abstract:
High-resolution X-ray and neutron crystallography were employed to elucidate redox-dependent structural changes in ferredoxin-NADP + reductase (FNR) from maize. This study focused on the rearrangement of hydrogen-bond networks upon FAD reduction. The X-ray structures of wild-type FNR in oxidized and reduced states were refined to 1.15 and 1.10 Å resolution, respectively, revealing no large structural changes in the main-chain backbones. Neutron crystallography provided complementary insights, confirming protonation at N1 and N5 of the isoalloxazine ring and visualizing hydrogen bonds that were undetectable by X-ray analysis. These findings illuminate the dynamic reorganization of water-mediated hydrogen-bond networks during redox transitions, which may underpin the redox-dependent modulation of partner binding by FNR. This integrated structural approach highlights the synergistic use of X-ray and neutron crystallography in studying redox-active proteins.
Organizational Affiliation:
Protein Crystallography Laboratory, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
