Oxidative modification of methionine80 in cytochrome c by reaction with peroxides
文献类型：期刊论文
| 作者 | Nugraheni, Ari Dwi2,3; Ren, Chunguang1,2,4; Matsumoto, Yorifumi2; Nagao, Satoshi2; Yamanaka, Masaru2; Hirota, Shun2 |
| 刊名 | JOURNAL OF INORGANIC BIOCHEMISTRY
 |
| 出版日期 | 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. |
| WOS关键词 | STRUCTURALLY ENGINEERED CYTOCHROMES ; COMPOUND I ; CARDIOLIPIN COMPLEX ; HYDROGEN-PEROXIDE ; MYOGLOBIN MUTANTS ; APOPTOSIS ; BINDING ; HEME ; MITOCHONDRIA ; SPECTROSCOPY |
| 资助项目 | JSPS[JP26288080] ; JSPS[JP16H00839] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Chemistry |
| 语种 | 英语 |
| WOS记录号 | WOS:000430157000022 |
| 出版者 | ELSEVIER SCIENCE INC |
| 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. |
入库方式： OAI收割
来源：上海药物研究所
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