中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Dimerization of hydroxylated species of m-aminophenol by cytochrome c with hydrogen peroxide

文献类型:期刊论文

作者Zhu YM ; Li JH ; Dong SJ
刊名journal of molecular catalysis b-enzymatic
出版日期1998
卷号5期号:5-6页码:475-482
关键词REACTIVE METABOLITES BILAYER-MEMBRANE OXYGENASES OXIDATION IRON
ISSN号1381-1177
通讯作者dong sj
中文摘要the cytochrome c and hydrogen peroxide-dependent oxidation of m-aminophenol was investigated by electrochemistry and spectrophotometry. the results indicated that the hydroxylated species of m-aminophenol have at least two conjugated substituted groups on the ring system (most possibly, its oxidized form 2-hydroxy-4-iminoquinone), and that the degradation of cytochrome c by hydrogen peroxide can also be prevented in the presence of m-aminophenol. the hydroxyl radical scavengers, mannitol and sodium benzoate, almost completely eliminate the hydroxylation of m-aminophenol. but oxo-heme species scavenger, uric acid, does not inhibit the hydroxylation. combining the results of mass spectrum, nuclear magnetic resonance and element analysis with that of spectrophotometry, electrochemistry and chemical scavengers, it is suggested that cytochrome c may act as a peroxidase, which facilitates the hydroxylation and subsequent dimerization of m-aminophenol. (c) 1998 elsevier science b.v. all rights reserved.
收录类别SCI收录期刊论文
语种英语
WOS记录号WOS:000077548300004
公开日期2010-11-04
源URL[http://202.98.16.49/handle/322003/22617]  
专题长春应用化学研究所_长春应用化学研究所知识产出_期刊论文
推荐引用方式
GB/T 7714
Zhu YM,Li JH,Dong SJ. Dimerization of hydroxylated species of m-aminophenol by cytochrome c with hydrogen peroxide[J]. journal of molecular catalysis b-enzymatic,1998,5(5-6):475-482.
APA Zhu YM,Li JH,&Dong SJ.(1998).Dimerization of hydroxylated species of m-aminophenol by cytochrome c with hydrogen peroxide.journal of molecular catalysis b-enzymatic,5(5-6),475-482.
MLA Zhu YM,et al."Dimerization of hydroxylated species of m-aminophenol by cytochrome c with hydrogen peroxide".journal of molecular catalysis b-enzymatic 5.5-6(1998):475-482.

入库方式: OAI收割

来源:长春应用化学研究所

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