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 Citations (Scopus)

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
Pages (from-to)239-244
Number of pages6
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume47
Issue number3-4
DOIs
Publication statusPublished - Apr 1 1992

Fingerprint

Proton-Translocating ATPases
Chloroplasts
Adenosine Triphosphate
Chemical activation
Hydrolysis
Chloroplast Proton-Translocating ATPases
Enzyme Activation
Energy Transfer
Enzymes
Liposomes
Energy transfer
Nucleotides
tentoxin

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Effect of Tentoxin on the Activation and on the Catalytic Reaction of Reconstituted H+-Atpase From Chloroplasts. / Fromme, Petra; Dahse, Ingo; Gräber, Peter.

In: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Vol. 47, No. 3-4, 01.04.1992, p. 239-244.

Research output: Contribution to journalArticle

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