An oxo-ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxidases trapped by microsecond freeze-hyperquenching (MHQ)

FEBS Letters
F G M WiertzS de Vries

Abstract

The pre-steady state reaction kinetics of the reduction of molecular oxygen catalyzed by fully reduced cytochrome oxidase from Escherichia coli and Paracoccus denitrificans were studied using the newly developed microsecond freeze-hyperquenching mixing-and-sampling technique. Reaction samples are prepared 60 and 200 micros after direct mixing of dioxygen with enzyme. Analysis of the reaction samples by low temperature UV-Vis spectroscopy indicates that both enzymes are trapped in the PM state. EPR spectroscopy revealed the formation of a mixture of two radicals in both enzymes. Based on its apparent g-value and lineshape, one of these radicals is assigned to a weakly magnetically coupled oxo-ferryl tryptophan cation radical. Implications for the catalytic mechanism of cytochrome oxidases are discussed.

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Citations

Jul 14, 2010·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Vasily S OganesyanAndrew J Thomson
Apr 24, 2009·Biochimica Et Biophysica Acta·Ville R I KailaMårten Wiström
Mar 10, 2009·Biochimica Et Biophysica Acta·Oliver-Matthias H Richter, Bernd Ludwig
Jul 2, 2011·Biochimica Et Biophysica Acta·Michelle A YuGary J Gerfen
Aug 30, 2006·Biochimica Et Biophysica Acta·Sergey A SiletskyRobert B Gennis
Mar 5, 2014·Chemical Reviews·Edward I SolomonLi Tian
Feb 8, 2006·FEBS Letters·Fraser MacMillanHartmut Michel
Sep 1, 2009·Metallomics : Integrated Biometal Science·Wilfred R Hagen
Dec 11, 2013·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Roberta PievoMarina Bennati
Jul 5, 2017·Scientific Reports·Rebecka AnderssonGisela Brändén
May 11, 2021·Biochimica Et Biophysica Acta. Bioenergetics·T SztachovaM Fabian
Nov 9, 2010·Chemical Reviews·Ville R I KailaMårten Wikström

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