Potentiometric analysis of Escherichia coli cytochromes in the optical absorbance range of 500 nm to 700 nm.
The oxidation-reduction potentials of Escherichia coli cytochromes have been studied by a recently described technique for automated electrodic potentiometry (Hendler, R.W., Songco, D., and Clem, T.R. (1977) Anal. Chem. 49, 1908-1913; Hendler, R.W. (1977) Anal. Chem. 49, 1914-1918), where entire spectra are recorded at a series of solution potentials. New techniques for resolution of the spectra versus voltage data have been applied. The results indicate that a 1-electron transport chain conducts electrons from substrate to cytochrome d, which is the cytochrome oxidase. Cytochrome d contains several components which appear to increase electron transfer first to a 2-electron stage and then to a 4-electron stage for the final reduction of a molecule of oxygen to 2 molecules of water.
D002462:Cell Membrane / Q000378:metabolism; D003580:Cytochromes; D004926:Escherichia coli / Q000032:analysis*; D005292:Ferricyanides; D008433:Mathematics; D008773:Methylphenazonium Methosulfate; D010084:Oxidation-Reduction; D011199:Potentiometry; D011485:Protein Binding; D011809:Quinones; D013053:Spectrophotometry
D003580:Cytochromes; D005292:Ferricyanides; D011809:Quinones; D008773:Methylphenazonium Methosulfate