TY - JOUR
T1 - Defining a direction
T2 - Electron transfer and catalysis in Escherichia coli complex II enzymes
AU - Maklashina, Elena
AU - Cecchini, Gary
AU - Dikanov, Sergei A.
N1 - Funding Information:
The work from the authors' laboratories was supported, in whole or in part by the Department of Veterans Affairs , Biomedical Laboratory Research and Development , and the National Institutes of Health Grant GM61606 (to G. Cecchini) and by the National Institutes of Health Grant GM62954 and Grant DE-FG02-08ER15960 from the Chemical Sciences, Geosciences and Biosciences Division, Office of Basic Energy Sciences, Office of Sciences, U.S. Department of Energy (to S.A. Dikanov), The authors gratefully acknowledge the critical reading of the manuscript and useful comments by Brian Ackrell and Alex Taguchi.
PY - 2013/5
Y1 - 2013/5
N2 - There are two homologous membrane-bound enzymes in Escherichia coli that catalyze reversible conversion between succinate/fumarate and quinone/quinol. Succinate:ubiquinone reductase (SQR) is a component of aerobic respiratory chains, whereas quinol:fumarate reductase (QFR) utilizes menaquinol to reduce fumarate in a final step of anaerobic respiration. Although, both protein complexes are capable of supporting bacterial growth on either minimal succinate or fumarate media, the enzymes are more proficient in their physiological directions. Here we evaluate factors that may underlie this catalytic bias. This article is part of a Special Issue entitled: Respiratory complex II: Role in cellular physiology and disease.
AB - There are two homologous membrane-bound enzymes in Escherichia coli that catalyze reversible conversion between succinate/fumarate and quinone/quinol. Succinate:ubiquinone reductase (SQR) is a component of aerobic respiratory chains, whereas quinol:fumarate reductase (QFR) utilizes menaquinol to reduce fumarate in a final step of anaerobic respiration. Although, both protein complexes are capable of supporting bacterial growth on either minimal succinate or fumarate media, the enzymes are more proficient in their physiological directions. Here we evaluate factors that may underlie this catalytic bias. This article is part of a Special Issue entitled: Respiratory complex II: Role in cellular physiology and disease.
KW - Complex II
KW - Iron sulfur cluster
KW - Protein electron transport
KW - Quinol:fumarate reductase
KW - Quinone binding site
KW - Succinate:quinone oxidoreductase
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U2 - 10.1016/j.bbabio.2013.01.010
DO - 10.1016/j.bbabio.2013.01.010
M3 - Review article
C2 - 23396003
AN - SCOPUS:84875722445
SN - 0005-2728
VL - 1827
SP - 668
EP - 678
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 5
ER -