Journal
BIOCHEMISTRY
Volume 47, Issue 38, Pages 9931-9933Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi8013483
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Funding
- National Institutes of Health [GM26916]
- Michigan Technology Tri Corridor Center for Structural Biology Core Technology Alliance [085P1000817]
- Michigan State University [03-016]
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Micromolar concentrations of the bile salt deoxycholate are shown to rescue the activity of an inactive mutant, E101A, in the K proton pathway of Rhodobacter sphaeroides cytochrome c oxidase. A crystal structure of the wild-type enzyme reveals, as predicted, deoxycholate bound with its carboxyl group at the entrance of the K path. Since cholate is a known potent inhibitor of bovine oxidase and is seen in a similar position in the bovine structure, the crystallographically defined, conserved steroid binding site could reveal a regulatory site for steroids or structurally related molecules that act on the, essential K proton path.
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