Redox induced protonation of heme propionates in cytochrome c oxidase: Insights from surface enhanced resonance Raman spectroscopy and QM/MM calculations
刊名:Biochimica et Biophysica Acta (BBA) - Bioenergetics
出版年:2017
出版时间:February 2017
年:2017
卷:1858
期:2
页码:103-108
全文大小:729 K
卷排序:1858
文摘
Successful immobilization of cytochrome c oxidase on electrodes allowed controlling the redox states of heme a and a3 The protonation states of the heme propionates were identified by comparing SERRS spectra with QM/MM calculations In the fully reduced enzyme at least three of the four propionates are protonated A deprotonated PrDa and protonated PrDa3 was observed concomitantly with a reduced heme a and an oxidized heme a3