Effect of Tentoxin on the Activation and on the Catalytic Reaction of Reconstituted H+-Atpase From Chloroplasts

Petra Fromme, Ingo Dahse, Peter Gräber

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

The proton-translocating ATPase from chloroplasts, CF0F1, was isolated, purified and reconstitutedinto asolectin liposomes. The effect of the energy transfer inhibitor, tentoxin, on different functions of the enzyme was investigated. Tentoxin does not inhibit the nucleotide release during energization by a pH Δψ jump, i.e. the activation of the enzyme is not influenced. ATP synthesis driven by a pH Δψ T jump and multi-site ATP hydrolysis are completely inhibited by tentoxin, whereas uni-site ATP hydrolysis is not influenced.

Original languageEnglish (US)
Pages (from-to)239-244
Number of pages6
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume47
Issue number3-4
DOIs
StatePublished - Apr 1 1992
Externally publishedYes

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Keywords

  • CFF
  • Enzyme Kinetics
  • H-ATPase
  • Tentoxin
  • Uni-Site Catalysis

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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