Localization of acidic residues involved in the proton pumping activity of the bovine heart mitochondrial bc1complex
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(99)00920-5/fullpdf
Reference32 articles.
1. [7] Ubiquinol-cytochrome-c reductase from human and bovine mitochondria
2. Crystal Structure of the Cytochrome bc 1 Complex from Bovine Heart Mitochondria
3. Electron transfer by domain movement in cytochrome bc1
4. Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
5. Characteristics of energy-linked proton translocation in liposome reconstituted bovine cytochrome bc1 complex. Influence of the protonmotive force on the H+/e- stoichiometry
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3. Aspartate-186 in the head group of the yeast iron–sulfur protein of the cytochrome bc1 complex contributes to the protein conformation required for efficient electron transfer;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2003-12
4. Carboxyl Residues in the Iron−Sulfur Protein Are Involved in the Proton Pumping Activity of P. denitrificans bc1 Complex;Biochemistry;2001-11-16
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