Is cytochrome b glutamic acid 272 a quinol binding residue in the bc1 complex of Saccharomyces cerevisiae?

Biochemistry
Nadir SeddikiGaël Brasseur

Abstract

The mitochondrial bc1 complex catalyzes the oxidation of ubiquinol and the reduction of cytochrome (cyt) c coupled to a vectorial translocation of protons across the membrane. On the basis of the three-dimensional structures of the bc1 complex in the presence of the inhibitor stigmatellin, it was assumed that the substrate quinol binding involves the cyt b glutamate residue E272 and the histidine 181 on the Rieske protein. Although extensive mutagenesis of glutamate E272 has been carried out, different experimental results were recently obtained, and different conclusions were drawn to explain its role in the bifurcated electron/proton transfer at the QO site. This residue is not totally conserved during evolution. We show in this study that replacement of E272 with apolar residues proline and valine naturally present in some organisms did not abolish the bc1 activity, although it slowed down the kinetics of electron transfer. The Km value for the binding of the substrate quinol was not modified, and the EPR data showed that the quinone/quinol binding still occurred in the mutants. Binding of stigmatellin was retained; however, mutations E272P,V induced resistance toward the QO site inhibitor myxothiazol. The pH dependence of t...Continue Reading

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Citations

Sep 30, 2010·The FEBS Journal·Cleverson BussoMario H Barros
Oct 28, 2015·The Journal of Physical Chemistry. B·Muhammad A HagrasAlexei A Stuchebrukhov
Nov 6, 2012·Biochimica Et Biophysica Acta·Doreen VictoriaAntony R Crofts
Feb 12, 2013·Biochimica Et Biophysica Acta·Antony R CroftsKlaus Schulten
Aug 13, 2014·Genome Biology and Evolution·Wei-Chun Kao, Carola Hunte
Mar 5, 2015·Human Molecular Genetics·Claudia NestiFilippo M Santorelli
Jun 30, 2021·Chemical Reviews·Peter BrzezinskiPia Ädelroth

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