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Dynamics of Membrane-Associated Energy-Transducing Catalysts. A Study with Mitochondrial Adenosine Triphosphatase Inhibitor

  • L. Ernster
  • K. Asami
  • K. Juntti
  • J. Coleman
  • K. Nordenbrand
Part of the Nobel Foundation Symposia book series (NOFS, volume 34)

Abstract

In recent years evidence has accumulated which strongly supports the concept that energy transfer between various membrane-associated energy-transducing units — electron-transport catalysts, ATP-synthesizing enzymes and ion-translocators of mitochondria, chloroplasts and prokaryotes — can take place via a transmembrane proton gradient and/or a membrane potential, in accordance with the chemiosmotic hypothesis of Mitchell (1961, 1966). The mechanisms by which such an electrochemical gradient is formed and utilized are not known but presumably involve the operation of proton pumps that are components — probably subunits — of the various energy-transducing units (cf. Ernster (1975) for review). It is also not known whether the formation of an electrochemical gradient by a given energy-transducing unit is the primary event of energy conservation, or whether it is preceded by a chemical — e.g. conformational — change that in turn gives rise to an electrochemical gradient. Furthermore, the question arises as to whether transmembrane electrochemical gradients are the sole way of interaction between energy-transducing units located in the same membrane, or whether there may also occur more direct interactions between such units. The purpose of this paper is to summarize experimental data obtained in our laboratory over the last few years in studies of the ATPase inhibitor of Pullman and Monroy (1963) that may be relevant to some of these problems.

Keywords

ATPase Inhibitor Mitochondrial ATPase ATPase Reaction Nicotinamide Nucleotide Transmembrane Proton Gradient 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

AI

ATPase inhibitor

ANS

8-anilino-naphthalene-1sulfonate

FCCP

carbonyl cyanide p-trifluoromethoxyphenylhydrazone

LDH

lactate dehydrogenase

PEP

phospho(enol)pyruvate

PK

pyruvate kinase

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • L. Ernster
    • 1
  • K. Asami
    • 1
  • K. Juntti
    • 1
  • J. Coleman
    • 1
  • K. Nordenbrand
    • 1
  1. 1.Department of BiochemistryArrhenius Laboratory University of StockholmStockholmSweden

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