Abstract

The mechanism and stoichiometry of proton transport by the respiratory chain of heart mitochondria and E. coli will be studied. The dependence of ATP synthesis, H2180-Pi exchange reactions, binding of the F1 inhibitor peptide, and conformational change of F1 on the membrane potential and pH gradient of submitochondrial particles will be measured. The effect of possible permeant acids and bases on proton transport measurements will be studied in liposomes. Proton transport by a simple NADH-CoQ reductase from E. coli will be studied in vesicles and a reconstituted system.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL014483-16
Application #
3334779
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1977-07-01
Project End
1988-09-30
Budget Start
1987-07-01
Budget End
1988-09-30
Support Year
16
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Cornell University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850

  Publications

Hinkle, P C; Kumar, M A; Resetar, A et al. (1991) Mechanistic stoichiometry of mitochondrial oxidative phosphorylation. Biochemistry 30:3576-82
Krishnamoorthy, G; Hinkle, P C (1988) Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase. J Biol Chem 263:17566-75