Oxidative modification of methionine80 in cytochrome c by reaction with peroxides

doi:10.1016/j.jinorgbio.2018.02.017

	Oxidative modification of methionine80 in cytochrome c by reaction with peroxides
	Nugraheni, Ari Dwi 2,3; Ren, Chunguang 1,2,4; Matsumoto, Yorifumi 2; Nagao, Satoshi 2; Yamanaka, Masaru 2; Hirota, Shun 2
刊名	JOURNAL OF INORGANIC BIOCHEMISTRY
	2018-05
卷号	182 页码:200-207
关键词	Cytochrome c Methionine oxidation Peroxidase reaction Self-modification
ISSN号	0162-0134
DOI	10.1016/j.jinorgbio.2018.02.017
文献子类	Article
英文摘要	The Met80-heme iron bond of cytochrome c (cyt c) is cleaved by the interaction of cyt c with cardiolipin (CL) in membranes. The Met80 dissociation enhances the peroxidase activity of cyt c and triggers cyt c release from mitochondrion to the cytosol at the early stage of apoptosis. This paper demonstrates the selective oxidation of Met80 for the reaction of ferric cyt c with a peroxide, meta-chloroperbenzoic acid (mCPBA), in the presence of CL-containing liposomes by formation of a ferryl species (Compound I). After the reaction of cyt c with mCPBA in the presence of 1,2-dioloeyl-sn-glycero-3-phosphocholine (DOPC) liposomes containing CL, the electrospray ionization mass spectrum of the peptide fragments, obtained by digestion of cyt c with lysyl endopeptidase, exhibited a peak at m/z = 795.45; whereas, this peak was not observed for the peptide fragments obtained after the reaction in the presence of DOPC liposomes not containing CL. According to the tandem mass spectrum of the m/z = 795.45 peptide fragment, Met80 was modified with a 16 Da mass increase. The purified Met80-modified cyt c exhibited a peroxidase activity more than 5-fold higher than that of the unmodified protein. Transient absorption bands around 650 nm were generated by the reactions with mCPBA for ferric wild-type cyt c in the presence of CL-containing DOPC liposomes and ferric Y67F cyt c in the absence of liposomes. The formation and decomposition rates of the 650-nm absorption species increased and decreased, respectively, by increasing the mCPBA concentration in the reaction, indicating transient formation of Compound I.
资助项目	JSPS[JP26288080] ; JSPS[JP16H00839]
WOS关键词	STRUCTURALLY ENGINEERED CYTOCHROMES ; COMPOUND I ; CARDIOLIPIN COMPLEX ; HYDROGEN-PEROXIDE ; MYOGLOBIN MUTANTS ; APOPTOSIS ; BINDING ; HEME ; MITOCHONDRIA ; SPECTROSCOPY
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry
语种	英语
出版者	ELSEVIER SCIENCE INC
WOS记录号	WOS:000430157000022
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/279783]
专题	中国科学院上海药物研究所
通讯作者	Hirota, Shun
作者单位	1.Chinese Acad Sci, Shanghai Inst Mat Med, Yantai Branch, 39 Keji Rd, Yantai 264000, Shandong, Peoples R China; 2.Nara Inst Sci & Technol, Grad Sch Mat Sci, 8916-5 Takayama, Nara 6300192, Japan; 3.Univ Gadjah Mada, Fac Math & Nat Sci, Dept Phys, Sekip Utara BLS 21, Yogyakarta 55281, Indonesia; 4.Yantai Inst Mat Med, 39 Keji Rd, Yantai 264000, Shandong, Peoples R China
推荐引用方式 GB/T 7714	Nugraheni, Ari Dwi,Ren, Chunguang,Matsumoto, Yorifumi,et al. Oxidative modification of methionine80 in cytochrome c by reaction with peroxides[J]. JOURNAL OF INORGANIC BIOCHEMISTRY,2018,182:200-207.
APA	Nugraheni, Ari Dwi,Ren, Chunguang,Matsumoto, Yorifumi,Nagao, Satoshi,Yamanaka, Masaru,&Hirota, Shun.(2018).Oxidative modification of methionine80 in cytochrome c by reaction with peroxides.JOURNAL OF INORGANIC BIOCHEMISTRY,182,200-207.
MLA	Nugraheni, Ari Dwi,et al."Oxidative modification of methionine80 in cytochrome c by reaction with peroxides".JOURNAL OF INORGANIC BIOCHEMISTRY 182(2018):200-207.