Article
Met23Lys mutation in subunit gamma of F(O)F(1)-ATP synthase from Rhodobacter capsulatus impairs the activation of ATP hydrolysis by protonmotive force.
Biochimica et biophysica acta - 1 Nov 2007
Feniouk Boris A, Rebecchi Alberto, Giovannini Donatella, Anefors Sofie, Mulkidjanian Armen Y, Junge Wolfgang, Turina Paola, Melandri B Andrea
Abstract excerpt
H(+)-F(O)F(1)-ATP synthase couples proton flow through its membrane portion, F(O), to the synthesis of ATP in its headpiece, F(1). Upon reversal of the reaction the enzyme functions as a proton pumping ATPase. Even in the simplest bacterial enzyme the ATPase activity is regulated by several mechanisms, involving inhibition by MgADP, conformational transitions of the epsilon subunit, and activation by protonmotive...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Amino Acid Substitution
- Bacterial Proton-Translocating ATPases
- Hydrolysis
- Kinetics
- Light
- Mutation
- Oxidation-Reduction
- Proton Pumps
- Proton-Motive Force
- Protons