Cell reports · 2023
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.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Wu Dong-Dong, Jin Sheng, Cheng Ruo-Xiao, Cai Wen-Jie, Xue Wen-Long, Zhang Qing-Qing, Yang Le-Jie, Zhu Qi, Li Meng-Yao, Lin Ge, Wang Yi-Zhen, Mu Xue-Pan, Wang Yu, Zhang Igor Ying, Zhang Qi, Chen Ying, Cai Sheng-Yang, Tan Bo, Li Ye, Chen Yun-Qian, Zhang Pu-Juan, Sun Chen, Yin Yue, Wang Ming-Jie, Zhu Yi-Zhun, Tao Bei-Bei, Zhou Jia-Hai, Huang Wei-Xue, Zhu Yi-Chun
Аннотация
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 (H2S), 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 H2S 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 H2S effect was also examined in both in vitro and in vivo models where the cardioprotective effects of H2S were dependent on Cu/Zn-SOD.