Product membrane-bound ATP synthase, Fo sector, subunit c; DCCD-binding-protein
| membrane-bound ATP synthase, Fo sector, subunit c; DCCD-binding-protein |
| Fo-ATPase, c-subunit |
| F1F0-type proton-ATPase/ATP synthase, c-subunit |
| DCCD-binding protein |
NULL
- Monticello, R.A., E. Angov, W.S. Brusilow 1992. Effects of inducing expression of cloned genes for the F0 proton channel of the Escherichia coli F1F0 ATPase. J.Bacteriol. 174:3370-3376
- Assadi-Porter, F.M., R.H. Fillingame 1995. Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR. Biochemistry 34:16186-16193
- Dmitriev, O.Y., R.H. Fillingame 2001. Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices. J.Biol.Chem. 276:27449-27454
- Suzuki, T., H. Ueno, N. Mitome, J. Suzuki, M. Yoshida 2002. F(0) of ATP synthase is a rotary proton channel.Obligatory coupling of proton translocation with rotation of c-subunit ring. J.Biol.Chem. 277:13281-13285
- Dmitriev, O.Y., F. Abildgaard, J.L. Markley, R.H. Fillingame 2002. Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex
- Arechaga, I., P.J. Butler, J.E. Walker 2002. Self-assembly of ATP synthase subunit c rings. FEBS Lett. 515:189-193