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Journal Abstract Search

119 related items for PubMed ID: 1385781

  • 1. The catalytic site is located on subunit I of the ATPase from Halobacterium saccharovorum. A direct photoaffinity labeling study.
    Bonet ML, Schobert B.
    Eur J Biochem; 1992 Jul 01; 207(1):369-76. PubMed ID: 1385781
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  • 9. ATP synthesis in Halobacterium saccharovorum: evidence that synthesis may be catalysed by an F0F1-ATP synthase.
    Hochstein LI.
    FEMS Microbiol Lett; 1992 Oct 01; 76(1-2):155-9. PubMed ID: 11537859
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  • 12. Bound adenosine 5'-triphosphate formation, bound adenosine 5'-diphosphate and inorganic phosphate retention, and inorganic phosphate oxygen exchange by chloroplast adenosinetriphosphatase in the presence of Ca2+ or Mg2+.
    Wu D, Boyer PD.
    Biochemistry; 1986 Jun 03; 25(11):3390-6. PubMed ID: 2873834
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  • 13. Mapping of nucleotide-depleted mitochondrial F1-ATPase with 2-azido-[alpha-32P]adenosine diphosphate. Evidence for two nucleotide binding sites in the beta subunit.
    Lunardi J, Garin J, Issartel JP, Vignais PV.
    J Biol Chem; 1987 Nov 05; 262(31):15172-81. PubMed ID: 2889735
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  • 14. Do ATP4- and Mg2+ bind stepwise to the F1-ATPase of Halobacterium saccharovorum?
    Schobert B.
    Eur J Biochem; 1998 Jun 01; 254(2):363-70. PubMed ID: 9660192
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  • 17. Adenine nucleotide binding at a noncatalytic site of mitochondrial F1-ATPase accelerates a Mg(2+)- and ADP-dependent inactivation during ATP hydrolysis.
    Murataliev MB.
    Biochemistry; 1992 Dec 29; 31(51):12885-92. PubMed ID: 1463756
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  • 18. Demonstration of two exchangeable non-catalytic and two cooperative catalytic sites in isolated bovine heart mitochondrial F1, using the photoaffinity labels [2-3H]8-azido-ATP and [2-3H]8-azido-ADP.
    van Dongen MB, Berden JA.
    Biochim Biophys Acta; 1986 Jun 10; 850(1):121-30. PubMed ID: 2871864
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  • 20. [Functions and localization of nucleotide-binding sites of CF1-ATPase using dialdehyde derivatives of ADP and ATP].
    Sytnik SK, Mal'ian AN.
    Biokhimiia; 1983 Jun 10; 48(6):890-6. PubMed ID: 6224516
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