The unusual enzymology of ATP synthase
- PMID: 2894841
- DOI: 10.1021/bi00400a001
The unusual enzymology of ATP synthase
Similar articles
-
Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit.Biochim Biophys Acta. 1984 Dec 17;768(3-4):201-8. doi: 10.1016/0304-4173(84)90016-8. Biochim Biophys Acta. 1984. PMID: 6239652 No abstract available.
-
Proton-conducting portion (F0) from Escherichia coli ATP synthase: preparation, dissociation into subunits, and reconstitution of an active complex.Methods Enzymol. 1986;126:569-78. doi: 10.1016/s0076-6879(86)26059-0. Methods Enzymol. 1986. PMID: 2908466 No abstract available.
-
Temperature-sensitive mutations at the carboxy terminus of the alpha subunit of the Escherichia coli F1F0 ATP synthase.J Bacteriol. 1991 Jul;173(14):4544-8. doi: 10.1128/jb.173.14.4544-4548.1991. J Bacteriol. 1991. PMID: 1829729 Free PMC article.
-
Rotational coupling in the F0F1 ATP synthase.Annu Rev Biophys Biomol Struct. 1999;28:205-34. doi: 10.1146/annurev.biophys.28.1.205. Annu Rev Biophys Biomol Struct. 1999. PMID: 10410801 Review.
-
ATP synthases. Structure, reaction center, mechanism, and regulation of one of nature's most unique machines.J Biol Chem. 1993 May 15;268(14):9937-40. J Biol Chem. 1993. PMID: 8486720 Review. No abstract available.
Cited by
-
Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme.Proc Natl Acad Sci U S A. 1989 Nov;86(22):8708-11. doi: 10.1073/pnas.86.22.8708. Proc Natl Acad Sci U S A. 1989. PMID: 2530585 Free PMC article.
-
The alpha 3 beta 3 complex, the catalytic core of F1-ATPase.Proc Natl Acad Sci U S A. 1989 Sep;86(17):6484-7. doi: 10.1073/pnas.86.17.6484. Proc Natl Acad Sci U S A. 1989. PMID: 2528144 Free PMC article.
-
Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy.Proc Natl Acad Sci U S A. 1990 Dec;87(24):9585-9. doi: 10.1073/pnas.87.24.9585. Proc Natl Acad Sci U S A. 1990. PMID: 2148209 Free PMC article.
-
Identification of subunits required for the catalytic activity of the F1-ATPase.J Bioenerg Biomembr. 1992 Oct;24(5):447-52. doi: 10.1007/BF00762361. J Bioenerg Biomembr. 1992. PMID: 1429538 Review.
-
Single-molecule analysis reveals rotational substeps and chemo-mechanical coupling scheme of Enterococcus hirae V1-ATPase.J Biol Chem. 2019 Nov 8;294(45):17017-17030. doi: 10.1074/jbc.RA119.008947. Epub 2019 Sep 13. J Biol Chem. 2019. PMID: 31519751 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources