Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase

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	Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase
	Lan, Wenxian 1; Wang, Zhonghua 2; Yang, Zhongzheng 1; Ying, Tianlei 2; Zhang, Xu 3; Tan, Xiangshi 2; Liu, Maili 3; Cao, Chunyang 1; Huang, Zhong-Xian 2
刊名	PLOS ONE
	2014-09-11
卷号	9 期号:9
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.
WOS标题词	Science & Technology
类目[WOS]	Multidisciplinary Sciences
研究领域[WOS]	Science & Technology - Other Topics
关键词[WOS]	ALKALINE CONFORMATIONAL TRANSITION ; YEAST ISO-1-CYTOCHROME-C ; HYDROGEN-PEROXIDE ; MET80X MUTANTS ; PROTEIN ; NMR ; RESOLUTION ; SPECTROSCOPY ; TYROSINE-67 ; VARIANT
收录类别	SCI
语种	英语
WOS记录号	WOS:000341855900059
公开日期	2015-07-14
内容类型	期刊论文
源URL	[http://ir.wipm.ac.cn/handle/112942/1494]
专题	武汉物理与数学研究所_磁共振基础研究部
作者单位	1.Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Nat Prod & Bioorgan Chem, Shanghai 200032, Peoples R China 2.Fudan Univ, Dept Chem, Biol Chem Lab, Shanghai 200433, Peoples R China 3.Chinese Acad Sci, Wuhan Inst Phys & Math, State Key Lab Magnet Resonance & Atom & Mol Phys, Wuhan, Peoples R China
推荐引用方式 GB/T 7714	Lan, Wenxian,Wang, Zhonghua,Yang, Zhongzheng,et al. Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase[J]. PLOS ONE,2014,9(9).
APA	Lan, Wenxian.,Wang, Zhonghua.,Yang, Zhongzheng.,Ying, Tianlei.,Zhang, Xu.,...&Huang, Zhong-Xian.(2014).Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase.PLOS ONE,9(9).
MLA	Lan, Wenxian,et al."Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase".PLOS ONE 9.9(2014).