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

Petra Fromme; Ingo Dahse; Peter Gräber

doi:10.1515/znc-1992-3-412

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 journal › Article › peer-review

15 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 language	English (US)
Pages (from-to)	239-244
Number of pages	6
Journal	Zeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume	47
Issue number	3-4
DOIs	https://doi.org/10.1515/znc-1992-3-412
State	Published - Apr 1 1992
Externally published	Yes

Keywords

CFF
Enzyme Kinetics
H-ATPase
Tentoxin
Uni-Site Catalysis

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

Access to Document

10.1515/znc-1992-3-412

Cite this

@article{b1d66804bd2d49c691fd68cb08e45445,

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

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.",

keywords = "CFF, Enzyme Kinetics, H-ATPase, Tentoxin, Uni-Site Catalysis",

author = "Petra Fromme and Ingo Dahse and Peter Gr{\"a}ber",

note = "Funding Information: We thank Dr. B. Liebermann, Jena, for his generous donation of tentoxin. This work was supported by the Deutsche Forschungsgemeinschaft (Sfb 312).",

year = "1992",

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language = "English (US)",

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T1 - Effect of Tentoxin on the Activation and on the Catalytic Reaction of Reconstituted H+-Atpase From Chloroplasts

AU - Fromme, Petra

AU - Dahse, Ingo

AU - Gräber, Peter

N1 - Funding Information: We thank Dr. B. Liebermann, Jena, for his generous donation of tentoxin. This work was supported by the Deutsche Forschungsgemeinschaft (Sfb 312).

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Y1 - 1992/4/1

N2 - 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.

AB - 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.

KW - CFF

KW - Enzyme Kinetics

KW - H-ATPase

KW - Tentoxin

KW - Uni-Site Catalysis

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