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学科主题: 生命有机化学
题名: Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase
其他题名: Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase
作者: Lan WX(蓝文贤)1; WANG ZHONGHUA1; YANG ZHONGZHENG1; YING TIANLEI1; ZHANG XU1; TAN XIANGSHI1; LIU MAILI1; Cao CY(曹春阳)1; HUANG ZHONGXIAN1
刊名: PLoS One
发表日期: 2014
DOI: 10.1371/journal.pone.0107305
卷: 9, 期:9, 页:e107305
收录类别: SCI
英文摘要: The catalytic activity of cytochrome c (cyt c) to peroxidize cardiolipin to its oxidized form is required for the release of proapoptotic factors from mitochondria, and for execution of the subsequent apoptotic steps. However, the structural basis for this peroxidation reaction remains unclear. In this paper, we determined the three-dimensional NMR solution structure of yeast cyt c Y67H variant with high peroxidase activity, which is almost similar to that of its native form. The structure reveals that the hydrogen bond between Met80 and residue 67 is disrupted. This change destabilizes the sixth coordination bond between heme Fe3+ ion and Met80 sulfur atom in the Y67H variant, and further makes it more easily be broken at low pH conditions. The steady-state studies indicate that the Y67H variant has the highest peroxidase activities when pH condition is between 4.0 and 5.2. Finally, a mechanism is suggested for the peroxidation of cardiolipin catalyzed by the Y67H variant, where the residue His67 acts as a distal histidine, its protonation facilitates O-O bond cleavage of H2O2 by functioning as an acidic catalyst.
语种: 英语
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/38954
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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作者单位: 1.中科院上海有机化学研究所
2.复旦大学
3.中科院武汉物理与数学研究所

Recommended Citation:
Lan WX,WANG ZHONGHUA,YANG ZHONGZHENG,et al. Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase[J]. PLoS One,2014,9(9):e107305.
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