Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins.
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins.
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系统 I 细胞色素 c 生物发生过程中的血红素运输和修饰：Ccm 蛋白血红素氧化还原潜力的见解。
DOI：
10.1021/acs.biochem.6b00427
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发表时间：
2016
期刊：
影响因子：
2.9
通讯作者：
Kranz,RobertG
中科院分区：
文献类型：
--
作者：
Sutherland,MollyC;Rankin,JoelA;Kranz,RobertG
Cytochromescrequire covalent attachment of heme via two thioether bonds at conserved CXXCH motifs, a process accomplished in prokaryotes by eight integral membrane proteins (CcmABCDEFGH), termed System I. Heme is trafficked from inside the cell to outside (via CcmABCD) and chaperoned (holoCcmE) to the cytochromecsynthetase (CcmF/H). Purification of key System I pathway intermediates allowed the determination of heme redox potentials. The data support a model whereby heme is oxidized to form holoCcmE and subsequently reduced by CcmF/H for thioether formation, with Fe2+being required for attachment to CXXCH. Results provide insight into mechanisms for the oxidation and reduction of hemein vivo.
