Membrane Topology of Subunit a of the F1F0 ATP Synthase as Determined by Labeling of Unique Cysteine Residues
Open Access
- 1 June 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (26) , 16235-16240
- https://doi.org/10.1074/jbc.273.26.16235
Abstract
No abstract availableKeywords
This publication has 69 references indexed in Scilit:
- Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coliFEBS Letters, 1996
- THE F0F1-TYPE ATP SYNTHASES OF BACTERIA: Structure and Function of the F0 ComplexAnnual Review of Microbiology, 1996
- Transmembrane topology of Escherichia coli H+‐ATPase (ATP synthase) subunit aFEBS Letters, 1996
- Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopyNature Structural & Molecular Biology, 1995
- The γ subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 partFEBS Letters, 1995
- Coupling between catalytic sites and the proton channel in F1F0-type ATPasesTrends in Biochemical Sciences, 1994
- Hairpin folding of subunit c of F1Fo ATP synthase: 1H distance measurements to nitroxide-derivatized aspartyl-61Biochemistry, 1994
- Membrane protein structure predictionJournal of Molecular Biology, 1992
- The transmembrane topology of the α subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusionsFEBS Letters, 1990
- The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984