PMID:11132627
| Citation |
Tsubaki, M, Hori, H and Mogi, T (2000) Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers. J. Inorg. Biochem. 82:19-25 |
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| Abstract |
Cytochromes bo and bd are structurally unrelated terminal ubiquinol oxidases in the aerobic respiratory chain of Escherichia coli. The high-spin heme o-CuB binuclear center serves as the dioxygen reduction site for cytochrome bo, and the heme b595-heme d binuclear center for cytochrome bd. CuB coordinates three histidine ligands and serves as a transient ligand binding site en route to high-spin heme o one-electron donor to the oxy intermediate, and a binding site for bridging ligands like cyanide. In addition, it can protect the dioxygen reduction site through binding of a peroxide ion in the resting state, and connects directly or indirectly Tyr288 and Glu286 to carry out redox-driven proton pumping in the catalytic cycle. Contrary, heme b595 of cytochrome bd participate a similar role to CuB in ligand binding and dioxygen reduction but cannot perform such versatile roles because of its rigid structure. |
| Links | |
| Keywords |
Binding Sites; Cytochromes/chemistry; Cytochromes/metabolism; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Electron Transport Complex IV/chemistry; Electron Transport Complex IV/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Ligands; Oxidation-Reduction; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Protein Structure, Quaternary |
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