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^*

^*Corresponding author for this work

University of Illinois at Urbana-Champaign

Research output: Contribution to journal › Article › peer-review

25 Citations (Scopus)

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-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.

Original language	English
Pages (from-to)	1174-1177
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	136
Issue number	4
DOIs	https://doi.org/10.1021/ja4091885
Publication status	Published - 29 Jan 2014
Externally published	Yes

Access to Document

10.1021/ja4091885

Cite this

@article{9117298db67c412489c898241deab34a,

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",

year = "2014",

month = jan,

day = "29",

doi = "10.1021/ja4091885",

language = "English",

volume = "136",

pages = "1174--1177",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "4",

}

TY - JOUR

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.

UR - http://www.scopus.com/inward/record.url?scp=84893451150&partnerID=8YFLogxK

U2 - 10.1021/ja4091885

DO - 10.1021/ja4091885

M3 - Article

C2 - 24383850

AN - SCOPUS:84893451150

SN - 0002-7863

VL - 136

SP - 1174

EP - 1177

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this