Dispensable residues in the active site of the cytochrome c biogenesis protein CcmH.
Dispensable residues in the active site of the cytochrome c biogenesis protein CcmH.
复制标题
细胞色素 c 生物发生蛋白 CcmH 活性位点中的可有可无的残基。
DOI:
10.1016/j.febslet.2008.07.052
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发表时间:
2008
期刊:
影响因子:
3.5
通讯作者:
Robertson IB
中科院分区:
文献类型:
--
作者:
Robertson IB
Cytochrome c maturation (CcmH) functions in the assembly of c-type cytochromes in the Escherichia coli periplasm. The conserved cysteine pair in the N-terminal of its two membrane-anchored periplasmic domains is thought to reduce the CXXCH motif of cytochromes c. The recent structure of Pseudomonas aeruginosa CcmH identified conserved residues that might be functionally important. We replaced with alanine the active-site cysteines of E. coli CcmH, as well as R42, S54, R63, and tested the effects on cytochrome c production anaerobically and aerobically. Unexpectedly, replacement of the conserved non-cysteine active-site residues had little effect, whilst the cysteines were required under aerobic, but not anaerobic, conditions. We confirmed that removal of the C-terminal tetratricopeptide-like domain does not, surprisingly, abolish assembly of cytochromes c.