Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases

FEBS Letters
G CecchiniSo Iwata

Abstract

The anaerobically expressed fumarate reductase and aerobically expressed succinate dehydrogenase from Escherichia coli comprise two different classes of succinate:quinone oxidoreductases (SQR), often termed respiratory complex II. The X-ray structures of both membrane-bound complexes have revealed that while the catalytic/soluble domains are structurally similar the quinone binding domains of the enzyme complexes are significantly different. These results suggest that the anaerobic and aerobic forms of complex II have evolved different mechanisms for electron and proton transfer in their respective membrane domains.

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Citations

Dec 16, 2003·The Journal of Biological Chemistry·Kayode S OyedotunBernard D Lemire
Jul 26, 2006·The Journal of Biological Chemistry·Victor W T ChengJoel H Weiner
Jul 10, 2013·The Journal of Biological Chemistry·Prashant K SinghTina M Iverson
Apr 15, 2008·Journal of Bacteriology·Hiromi TakaradaShigeaki Harayama
Apr 24, 2012·The FEBS Journal·Poonam SharmaMartijn Bekker
Jun 16, 2012·Microbiology·Pedro M F SousaAna M P Melo
May 6, 2010·Future Microbiology·Vincent MeuricMartine Bonnaure-Mallet
May 9, 2012·Biochimica Et Biophysica Acta·Rodrigo Arias-CartinAxel Magalon
Jun 6, 2021·Biochimica Et Biophysica Acta. Proteins and Proteomics·Li-Shar HuangEdward A Berry
Mar 29, 2007·The Journal of Physical Chemistry. B·Sam HayCecilia Tommos
May 24, 2011·Journal of Proteomics·Jiri DreslerJiri Stulik

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