The raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunit.
Cooley, Jason W
The raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunit. [electronic resource] - Biochemistry Mar 2004 - 2217-27 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi035938u doi
Alanine--genetics
Benzoquinones--chemistry
Cell Membrane--enzymology
Electron Spin Resonance Spectroscopy
Electron Transport Complex III--antagonists & inhibitors
Enzyme Stability--genetics
Hydrogen Bonding
Hydroquinones--chemistry
Iron-Sulfur Proteins--chemistry
Mutagenesis, Site-Directed
Oxidation-Reduction
Polyenes--pharmacology
Potentiometry
Protein Structure, Tertiary--genetics
Protein Subunits--chemistry
Rhodobacter capsulatus--drug effects
The raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunit. [electronic resource] - Biochemistry Mar 2004 - 2217-27 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi035938u doi
Alanine--genetics
Benzoquinones--chemistry
Cell Membrane--enzymology
Electron Spin Resonance Spectroscopy
Electron Transport Complex III--antagonists & inhibitors
Enzyme Stability--genetics
Hydrogen Bonding
Hydroquinones--chemistry
Iron-Sulfur Proteins--chemistry
Mutagenesis, Site-Directed
Oxidation-Reduction
Polyenes--pharmacology
Potentiometry
Protein Structure, Tertiary--genetics
Protein Subunits--chemistry
Rhodobacter capsulatus--drug effects