The Quinone-binding Site in Succinate-ubiquinone Reductase fromEscherichia coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Proteins of the Inner Membrane of Escherichia coli : Identification of Succinate Dehydrogenase by Polyacrylamide Gel Electrophoresis with sdh Amber Mutants
2. One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556
3. Identification of the axial heme ligands of cytochromeb556in succinate: Ubiquinone oxidoreductase fromEscherichia coli
4. Two Hydrophobic Subunits Are Essential for the Heme b Ligation and Functional Assembly of Complex II (Succinate-Ubiquinone Oxidoreductase) from Escherichia coli
5. Localization of Histidine Residues Responsible for Heme Axial Ligation in Cytochrome b556 of Complex II (Succinate:Ubiquinone Oxidoreductase) in Escherichia coli
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