PMID:3040093
| Citation |
Hata-Tanaka, A, Matsuura, K, Itoh, S and Anraku, Y (1987) Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli. Biochim. Biophys. Acta 893:289-95 |
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| Abstract |
The ESR signals of the cytochromes in the Escherichia coli terminal oxidase cytochrome d complex were studied at cryogenic temperature. The intensities and g values of the rhombic high-spin signals changed when the electronic state of cytochrome d was changed from the oxidized state to the reduced or oxygen-binding or CO-binding state. These rhombic signals were therefore assigned to cytochrome b-595, which is located near cytochrome d in the oxidase complex. This assignment was supported by the finding that the Em value of the rhombic signals differed from that of cytochrome d (Hata, A. et al. (1985) Biochim. Biophys. Acta 810, 62-72). Photolysis and ligand-exchange experiments with the reduced CO complex of the oxidase were performed in the presence of oxygen at -140 degrees C. The ESR spectra of three intermediate forms trapped by controlled low temperatures were detected. These forms were designated as the oxygen-binding intermediate I (ESR-silent), oxygen-binding intermediate II (giving ESR signals at g = 6.3, 5.5 and 2.15), and oxygen-binding intermediate III (giving signals at g = 6.3, 5.5 and 6.0). From these results, electron flow in the cytochrome d complex is proposed to proceed in the order, cytochrome b-558----cytochrome b-595----cytochrome d----O2. A model of the mechanism of four-electron chemistry for oxidation of ubiquinol-8 and formation of H2O by the cytochrome d complex is presented. |
| Links | |
| Keywords |
Bacterial Proteins/metabolism; Carbon Monoxide/metabolism; Cytochrome b Group/metabolism; Cytochromes/metabolism; Cytochromes a1; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli/enzymology; Escherichia coli Proteins; Heme/metabolism; Multienzyme Complexes/metabolism; NADPH Oxidase; Oxidation-Reduction; Oxidoreductases/metabolism; Oxygen/metabolism; Protein Binding; Ubiquinone/analogs & derivatives; Ubiquinone/metabolism |
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