Redox induced protonation of heme propionates in cytochrome c oxidase: Insights from surface enhanced resonance Raman spectroscopy and QM/MM calculations

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• 作者：Murat Sezer^a ; Anna-Lena Woelke^b ; Ernst Walter Knapp^b ; Ramona Schlesinger^c ; Maria Andrea Mroginski^a ; ; Inez M. Weidinger^a ;
• 关键词：Cytochrome c oxidase ; Proton pumping ; Proton loading site ; Surface enhanced Raman spectroscopy ; 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