A conserved lysine residue controls iron–sulfur cluster redox chemistry in Escherichia coli fumarate reductase-Reference-Cited by-同舟云学术

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A conserved lysine residue controls iron–sulfur cluster redox chemistry in Escherichia coli fumarate reductase

Published:2013-10 Issue:10 Volume:1827 Page:1141-1147
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Cheng Victor W.T.,Tran Quang M.,Boroumand Nasim,Rothery Richard A.,Maklashina Elena,Cecchini Gary,Weiner Joel H.

Funder

Canadian Institutes of Health Research

National Institutes of Health

Department of Veterans Affairs, Office of Research and Development, Biomedical Laboratory Research Division

Canada Foundation for Innovation

Alberta Heritage Foundation for Medical Research

Canadian Institutes of Health Research Graduate Studentships

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference48 articles.

1. Structure of the Escherichia coli fumarate reductase respiratory complex;Iverson;Science,1999

2. Crystallographic studies of the Escherichia coli quinol–fumarate reductase with inhibitors bound to the quinol-binding site;Iverson;J. Biol. Chem.,2002

3. Architecture of succinate dehydrogenase and reactive oxygen species generation;Yankovskaya;Science,2003

4. Succinate dehydrogenase and fumarate reductase from Escherichia coli;Cecchini;Biochim. Biophys. Acta,2002

5. The quinone-binding and catalytic site of complex II;Maklashina;Biochim. Biophys. Acta,2010

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