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Radical formation at tyr39 and tyr153 following reaction of yeast cytochrome C peroxidase with hydrogen peroxide.

机译:酵母细胞色素C过氧化物酶与过氧化氢反应后,在tyr39和tyr153处形成自由基。

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摘要

The formation of yeast cytochrome c peroxidase (CcP) compound I has been recognized for many years to be associated with formation of two protein-centered radicals. One of these radical sites is located at Trp191 and is directly involved in catalytic oxidation of ferrocytochrome c (Sivaraja, M., Goodin, D. B., Smith, M., Hoffman, B. M. (1989) Science 245, 738-740). The second radical has been proposed to arise from one or more tyrosyl residues of CcP. However, the tyrosyl residue (or residues) capable of forming this radical has not been identified, and the functional role of this radical remains poorly understood. In the present work, this issue has been addressed through the combined use of the spin-trapping reagent 2-methyl-2-nitrosopropane and peptide mapping by electrospray mass spectrometry to identify Tyr39 and Tyr153 as two tyrosyl residues that are capable of forming radical centers upon reaction of CcP with hydrogen peroxide. The implications of this observation to the catalytic mechanism of CcP are addressed with reference to the three-dimensional structure of CcP.
机译:酵母细胞色素c过氧化物酶(CcP)化合物I的形成已被公认多年与形成两个以蛋白质为中心的自由基有关。这些自由基位点之一位于Trp191,并且直接参与铁细胞色素c的催化氧化(Sivaraja,M.,Goodin,D. B.,Smith,M.,Hoffman,B.M.(1989)Science 245,738-740)。已经提出第二个自由基来自CcP的一个或多个酪氨酰基残基。然而,尚未鉴定出能够形成该自由基的酪氨酰基残基(一个或多个),并且对该自由基的功能作用仍然知之甚少。在本工作中,此问题已通过结合使用自旋捕获剂2-甲基-2-亚硝基丙烷和通过电喷雾质谱进行肽图分析来鉴定Tyr39和Tyr153为两个能够形成自由基中心的酪氨酰基残基CcP与过氧化氢反应后。参考CcP的三维结构,可以解决此观察对CcP催化机理的影响。

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