The α1-Helix in the Extra-Membranous Domain Contributes to the Stability of the Iron–Sulfur Protein of the Cytochrome bc1Complex
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. The Protonmotive Q Cycle in Mitochondria and Bacteria
2. Heterologous Complementation of a Rieske Iron-Sulfur Protein-deficient by the Gene of
3. Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain
4. Purification of a reconstitutively active iron-sulfur protein (oxidation factor) from succinate . cytochrome c reductase complex of bovine heart mitochondria.
5. ENERGY TRANSDUCTION BY CYTOCHROME COMPLEXES IN MITOCHONDRIAL AND BACTERIAL RESPIRATION: The Enzymology of Coupling Electron Transfer Reactions to Transmembrane Proton Translocation
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Mutations in the tether region of the iron–sulfur protein affect the activity and assembly of the cytochrome bc1 complex of yeast mitochondria;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-02
2. The role of various domains of the iron-sulfur protein in the assembly and activity of the cytochrome bc(1) complex of yeast mitochondria;Journal of Bioenergetics and Biomembranes;1999
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