18 research outputs found
Diagnostic imaging of abnormalities in the location of the spleen and in the number of spleens
In vitro study of human mutL homolog 1 hypermethylation in inducing drug resistance of esophageal carcinoma
Limited liability and the risk–incentive relationship
Moral hazard, Limited liability, Risk–incentive relationship, D82, D86,
The effect of green tea on blood pressure and lipid profile: A systematic review and meta-analysis of randomized clinical trials
Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis
In the mycobacterial electron-transport chain, respiratory complex III passes electrons from menaquinol to complex IV, which in turn reduces oxygen, the terminal acceptor. Electron transfer is coupled to transmembrane proton translocation, thus establishing the electrochemical proton gradient that drives ATP synthesis. We isolated, biochemically characterized, and determined the structure of the obligate III2IV2 supercomplex from Mycobacterium smegmatis, a model for Mycobacterium tuberculosis. The supercomplex has quinol:O-2 oxidoreductase activity without exogenous cytochrome c and includes a superoxide dismutase subunit that may detoxify reactive oxygen species produced during respiration. We found menaquinone bound in both the Q(o) and Q(i) sites of complex III. The complex III-intrinsic diheme cytochrome cc subunit, which functionally replaces both cytochrome c(1) and soluble cytochrome c in canonical electron-transport chains, displays two conformations: one in which it provides a direct electronic link to complex IV and another in which it serves as an electrical switch interrupting the connection.</p
