PMID:8663126
| Citation |
Saiki, K, Nakamura, H, Mogi, T and Anraku, Y (1996) Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. J. Biol. Chem. 271:15336-40 |
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| Abstract |
Subunit IV of the Escherichia coli bo-type ubiquinol oxidase is a 12-kDa membrane protein encoded by the cyoD gene and is conserved in the bacterial heme-copper terminal oxidases. To probe the functional role of subunit IV, we carried out deletion analysis and chemical cross-linking experiments with a homobifunctional and cleavable reagent. Spectroscopic properties of the mutant oxidases suggest that the C-terminal two-third (Val45 to His109) containing helices II and III is essential for the functional expression of the oxidase complex and for the CuB binding to the heme-copper binuclear center in subunit I. Cross-linking studies indicate that subunit IV is in close vicinity to subunit III. Based on these observations, we propose that subunit IV is present in a cleft formed by subunits I and III and assists the CuB binding to subunit I during biosynthesis or assembly of the oxidase complex. |
| Links | |
| Keywords |
Amino Acid Sequence; Catalysis; Cross-Linking Reagents; Electron Transport Complex IV/chemistry; Electron Transport Complex IV/metabolism; Escherichia coli/enzymology; Macromolecular Substances; Molecular Sequence Data; Recombinant Proteins; Sequence Deletion; Structure-Activity Relationship |
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