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This is the second of the pair of programmes on oxidative phosphorylation. Dr. Schatz explains the chemiosmotic hypothesis in detail and explores some of the current ideas about how ATP is synthesi...sed by an enzyme located in the inner membrane of the mitochondrion.
Metadata describing this Open University video programme
Module code and title: S322, Biochemistry and molecular biology
Item code: S322; 09
First transmission date: 23-03-1977
Published: 1977
Rights Statement:
Restrictions on use:
Duration: 00:24:29
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Producer: Jean Nunn
Contributor: Gottfried Schatz
Publisher: BBC Open University
Keyword(s): ATP; Binding site; Chemiosmotic hypothesis; Conformational change; Halobacter halobium; Mitochondrion; Oligomycin; Proton gradient; Purple membrane; Sub-mitochondrial particles
Footage description: Gottfried Schatz, with a high resolution molecular model of mitochondria membrane, introduces the programme. Schatz lists four key points of the chemiosmotic hypothesis. Animated diagrams help to illustrate his points. Schatz introduces an experiment which demonstrates that respiring mitochondria secrete protons. Film of the experiment in progress. A pen recorder plots the acidification of the suspending medium. An uncoupler is added to the solution and respiration stops. Schatz explains how Efraim Racker and his team discovered, in 1960, the crucial role of mitochondrial ATPase in oxidative phosphorylation. Animated diagrams and a model of mitochondrial membrane illustrate points made. Schatz goes to examine, using a model, the ATPase complex. He looks at its structure and then it's function in the context of the chemiosmotic hypothesis. Schatz explains how Racker isolated purified ATPase molecules and incorporated them into artificial phospholipid bilayers. Efraim Racker tells of the experiment he performed with bacteriorhodopsin which showed that after ATPase molecules were incorporated into artificial vessels they used a proton gradient to synthesise ATP. Shatz presents the view of Peter Mitchell (one of two conflicting views) on the mechanism by which mitochondrial ATPase uses the free energy of a proton gradient to synthesise ATP. Animated diagrams help to make his points. Schatz goes on to present the other view, that of Prof. Boyer, the essence of which is that the energy is used not to make ATP but to release it from its binding site on the ATPase enzyme. Animated diagrams help to illustrate points made. Schatz sums up the programme.
Master spool number: 6HT/72436
Production number: 00525_1265
Videofinder number: 1015
Available to public: no