8IQ0

Crystal structure of hydrogen sulfide-bound superoxide dismutase in oxidized state

8IQ0 の概要

• エントリーDOI: 10.2210/pdb8iq0/pdb
• 分子名称: Superoxide dismutase [Cu-Zn], COPPER (II) ION, ZINC ION, ... (9 entities in total)
• 機能のキーワード: dimer, oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 251846.08

構造登録者

Zhou, J.H.,Huang, W.X.,Cheng, R.X.,Zhang, P.J.,Zhu, Y.C. (登録日: 2023-03-15, 公開日: 2023-09-06)

主引用文献

Wu, D.D.,Jin, S.,Cheng, R.X.,Cai, W.J.,Xue, W.L.,Zhang, Q.Q.,Yang, L.J.,Zhu, Q.,Li, M.Y.,Lin, G.,Wang, Y.Z.,Mu, X.P.,Wang, Y.,Zhang, I.Y.,Zhang, Q.,Chen, Y.,Cai, S.Y.,Tan, B.,Li, Y.,Chen, Y.Q.,Zhang, P.J.,Sun, C.,Yin, Y.,Wang, M.J.,Zhu, Y.Z.,Tao, B.B.,Zhou, J.H.,Huang, W.X.,Zhu, Y.C.
Hydrogen sulfide functions as a micro-modulator bound at the copper active site of Cu/Zn-SOD to regulate the catalytic activity of the enzyme.
Cell Rep, 42:112750-112750, 2023

PubMed Abstract: The present study examines whether there is a mechanism beyond the current concept of post-translational modifications to regulate the function of a protein. A small gas molecule, hydrogen sulfide (HS), was found to bind at active-site copper of Cu/Zn-SOD using a series of methods including radiolabeled binding assay, X-ray absorption near-edge structure (XANES), and crystallography. Such an HS binding enhanced the electrostatic forces to guide the negatively charged substrate superoxide radicals to the catalytic copper ion, changed the geometry and energy of the frontier molecular orbitals of the active site, and subsequently facilitated the transfer of an electron from the superoxide radical to the catalytic copper ion and the breakage of the copper-His61 bridge. The physiological relevance of such an HS effect was also examined in both in vitro and in vivo models where the cardioprotective effects of HS were dependent on Cu/Zn-SOD.

PubMed: 37421623
DOI: 10.1016/j.celrep.2023.112750

実験手法

X-RAY DIFFRACTION (1.88 Å)