Correlations of Structure and Function in H+ Translocating Subunit c of F1F0 ATP Synthasea
- 1 November 1992
- journal article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 671 (1), 323-334
- https://doi.org/10.1111/j.1749-6632.1992.tb43806.x
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff baseBiochemistry, 1991
- Structure and Mechanism of F 0 F 1 ‐Type ATP Synthases and ATPasesPublished by Wiley ,1991
- Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesiclesBiochemistry, 1990
- The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained.Proceedings of the National Academy of Sciences, 1990
- Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopyBiochemistry, 1990
- Orientation of subunit c of the ATP synthase of Escherichia coli — a study with peptide-specific antibodiesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1990
- Organization of the F0 sector of Escherichia coli proton-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membraneBiochemistry, 1989
- Fo portion of Escherichia coli ATP synthase: orientation of subunit c in the membraneBiochemistry, 1987
- Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phaseBiochimie, 1986
- Identification of Amino‐Acid Substitutions in the Proteolipid Subunit of the ATP Synthase from Dicyclohexylcarbodiimide‐Resistant Mutants of Escherichia coliEuropean Journal of Biochemistry, 1980