Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286.
Mutants that decouple the proton pump of cytochrome c oxidase from Rhodobacter sphaeroides are postulated to do so by increasing the pK(a) of glutamate 286, which is 20 Angstrom away. The possibility that a conformational change near E286 is induced by the decoupling mutations (N139D and N207D) was investigated by FTIR difference spectroscopy. In both decoupled mutants, the reduced-minus-oxidized FTIR difference spectra show a shift of 2 cm(-1) to lower frequency of the band resulting from the absorbance of E286 in the oxidized enzyme. The decoupling mutants may influence E286 by altering the chain of water molecules which runs from the site of the mutations to E286.
Vakkasoglu
Ahmet S
AS
Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Morgan
Joel E
JE
Han
Dan
D
Pawate
Ashtamurthy S
AS
Gennis
Robert B
RB
D003576:Electron Transport Complex IV / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018698:Glutamic Acid / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017494:Proton Pumps / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D017550:Spectroscopy, Fourier Transform Infrared
D017494:Proton Pumps; D018698:Glutamic Acid; D003576:Electron Transport Complex IV