Electron-proton coupling in cytochrome c studied using protein variants.
An NMR study of the cytochrome c variant Asn52Ile is used to show how the redox state change in native cytochrome c is coupled to a rearrangement of a proton network which runs through the cytochrome c molecule. The substitution breaks the H-bond network and removes the coupling. The uncovering of this putative proton channel and the connection of changes to it with redox state changes of the iron centre of the protein allows a possible description of the way in which redox energy state changes can be coupled to energization and gating of protons in membranes.
Inorganic Chemistry Laboratory, University of Oxford, England.
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Y
Gao
G
G
McLendon
G J
GJ
Pielak
R J
RJ
Williams
D000595:Amino Acid Sequence; D001216:Asparagine / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D007473:Ion Channels / Q000737:chemistry; D007532:Isoleucine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009154:Mutation; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011522:Protons; D012441:Saccharomyces cerevisiae / Q000737:chemistry
D003574:Cytochrome c Group; D007473:Ion Channels; D011522:Protons; D007532:Isoleucine; D001216:Asparagine