Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions

Yang Yu; Arnab Mukherjee; Mark J. Nilges; Parisa Hosseinzadeh; Kyle D. Miner; Yi Lu

doi:10.1021/ja4091885

Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H₂O₂ and O₂ reactions

Yang Yu, Arnab Mukherjee, Mark J. Nilges, Parisa Hosseinzadeh, Kyle D. Miner, Yi Lu^*

^*此作品的通讯作者

University of Illinois at Urbana-Champaign

科研成果: 期刊稿件 › 文章 › 同行评审

25 引用（Scopus）

摘要

Tyrosine is a conserved redox-active amino acid that plays important roles in heme-copper oxidases (HCO). Despite the widely proposed mechanism that involves a tyrosyl radical, its direct observation under O₂ reduction conditions remains elusive. Using a functional oxidase model in myoglobin called F33Y-Cu_BMb that contains an engineered tyrosine, we report herein direct observation of a tyrosyl radical during both reactions of H ₂O₂ with oxidized protein and O₂ with reduced protein by electron paramagnetic resonance spectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.

源语言	英语
页（从-至）	1174-1177
页数	4
期刊	Journal of the American Chemical Society
卷	136
期	4
DOI	https://doi.org/10.1021/ja4091885
出版状态	已出版 - 29 1月 2014
已对外发布	是

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title = "Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions",

abstract = "Tyrosine is a conserved redox-active amino acid that plays important roles in heme-copper oxidases (HCO). Despite the widely proposed mechanism that involves a tyrosyl radical, its direct observation under O2 reduction conditions remains elusive. Using a functional oxidase model in myoglobin called F33Y-CuBMb that contains an engineered tyrosine, we report herein direct observation of a tyrosyl radical during both reactions of H 2O2 with oxidized protein and O2 with reduced protein by electron paramagnetic resonance spectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.",

author = "Yang Yu and Arnab Mukherjee and Nilges, {Mark J.} and Parisa Hosseinzadeh and Miner, {Kyle D.} and Yi Lu",

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T1 - Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions

AU - Yu, Yang

AU - Mukherjee, Arnab

AU - Nilges, Mark J.

AU - Hosseinzadeh, Parisa

AU - Miner, Kyle D.

AU - Lu, Yi

PY - 2014/1/29

Y1 - 2014/1/29

N2 - Tyrosine is a conserved redox-active amino acid that plays important roles in heme-copper oxidases (HCO). Despite the widely proposed mechanism that involves a tyrosyl radical, its direct observation under O2 reduction conditions remains elusive. Using a functional oxidase model in myoglobin called F33Y-CuBMb that contains an engineered tyrosine, we report herein direct observation of a tyrosyl radical during both reactions of H 2O2 with oxidized protein and O2 with reduced protein by electron paramagnetic resonance spectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.

AB - Tyrosine is a conserved redox-active amino acid that plays important roles in heme-copper oxidases (HCO). Despite the widely proposed mechanism that involves a tyrosyl radical, its direct observation under O2 reduction conditions remains elusive. Using a functional oxidase model in myoglobin called F33Y-CuBMb that contains an engineered tyrosine, we report herein direct observation of a tyrosyl radical during both reactions of H 2O2 with oxidized protein and O2 with reduced protein by electron paramagnetic resonance spectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.

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VL - 136

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 4

ER -

Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions

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Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H₂O₂ and O₂ reactions