4.4 Article

A conserved steroid binding site in cytochrome c oxidase

Journal

BIOCHEMISTRY
Volume 47, Issue 38, Pages 9931-9933

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/bi8013483

Keywords

-

Funding

  1. National Institutes of Health [GM26916]
  2. Michigan Technology Tri Corridor Center for Structural Biology Core Technology Alliance [085P1000817]
  3. Michigan State University [03-016]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available