Subunit Structure and Organization of the Genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Gö1
Open Access
- 1 August 1996
- journal article
- research article
- Published by Elsevier
- Vol. 271 (31), 18843-18852
- https://doi.org/10.1074/jbc.271.31.18843
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Delta mu Na+ drives the synthesis of ATP via an delta mu Na(+)-translocating F1F0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Gö1Journal of Bacteriology, 1994
- Properties Of The Plasma Membrane Atpases Of The Halophilic Archaebacteria Haloferax Mediterranei And Haloferax VolcaniiZeitschrift für Naturforschung C, 1992
- F-type or V-type? The chimeric nature of the archaebacterial ATP synthaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1992
- The ATP synthase of Halobacterium salinarium (halobium) is an archaebacterial type as revealed from the amino acid sequences of its two major subunitsArchives of Biochemistry and Biophysics, 1991
- Chemiosmotic energy conversion and the membrane ATPase of Methanolobus tindariusEuropean Journal of Biochemistry, 1990
- Chemiosmotic energy conversion of the archaebacterial thermoacidophile Sulfolobus acidocaldarius: oxidative phosphorylation and the presence of an F0-related N,N'-dicyclohexylcarbodiimide-binding proteolipidJournal of Bacteriology, 1989
- Dicyclohexylcarbodiimide-binding protein is a subunit of the Methanosarcina barkeri ATPase complexBiochemical and Biophysical Research Communications, 1989
- Amino Acid Sequence of the α and β Subunits of Methanosarcina barkeri ATPase Deduced from Cloned GenesPublished by Elsevier ,1989
- Archaebacterial ATPase: Studies on Subunit Composition and Quaternary Structure of the F1- Analogous ATPase fromSulfolobus acidocaldariusBiological Chemistry Hoppe-Seyler, 1988
- The purification and subunit structure of a membrane-bound ATPase from the archaebacterium Halobacterium saccharovorumBiochemical and Biophysical Research Communications, 1987