{"title":"Yeast cytochrome c peroxidase: mechanistic studies via protein engineering","authors":"James E. Erman, Lidia B. Vitello","doi":"10.1016/S0167-4838(02)00317-5","DOIUrl":null,"url":null,"abstract":"<div><p>Cytochrome <em>c</em> peroxidase (CcP) is a yeast mitochondrial enzyme that catalyzes the reduction of hydrogen peroxide to water by ferrocytochrome <em>c</em><span>. It was the first heme enzyme<span> to have its crystallographic structure determined and, as a consequence, has played a pivotal role in developing ideas about structural control of heme protein<span> reactivity. Genetic engineering of the active site of CcP, along with structural, spectroscopic, and kinetic characterization of the mutant proteins has provided considerable insight into the mechanism of hydrogen peroxide activation, oxygen–oxygen bond cleavage, and formation of the higher-oxidation state intermediates in heme enzymes. The catalytic mechanism involves complex formation between cytochrome </span></span></span><em>c</em> and CcP. The cytochrome <em>c</em>/CcP system has been very useful in elucidating the complexities of long-range electron transfer in biological systems, including protein–protein recognition, complex formation, and intracomplex electron transfer processes.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2002-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00317-5","citationCount":"92","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0167483802003175","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 92
Abstract
Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme that catalyzes the reduction of hydrogen peroxide to water by ferrocytochrome c. It was the first heme enzyme to have its crystallographic structure determined and, as a consequence, has played a pivotal role in developing ideas about structural control of heme protein reactivity. Genetic engineering of the active site of CcP, along with structural, spectroscopic, and kinetic characterization of the mutant proteins has provided considerable insight into the mechanism of hydrogen peroxide activation, oxygen–oxygen bond cleavage, and formation of the higher-oxidation state intermediates in heme enzymes. The catalytic mechanism involves complex formation between cytochrome c and CcP. The cytochrome c/CcP system has been very useful in elucidating the complexities of long-range electron transfer in biological systems, including protein–protein recognition, complex formation, and intracomplex electron transfer processes.
细胞色素c过氧化物酶(Cytochrome c peroxidase, CcP)是一种酵母线粒体酶,它催化铁细胞色素c将过氧化氢还原为水。它是第一个确定其晶体结构的血红素酶,因此在发展血红素蛋白反应性的结构控制方面发挥了关键作用。CcP活性位点的基因工程,以及突变蛋白的结构、光谱和动力学表征,为血红素酶中过氧化氢活化、氧-氧键裂解和高氧化态中间体形成的机制提供了相当大的见解。催化机制涉及细胞色素c与CcP之间形成复合物。细胞色素c/CcP系统在阐明生物系统中远程电子转移的复杂性方面非常有用,包括蛋白质-蛋白质识别、复合物形成和复合物内电子转移过程。