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PMID: 29710952 Published · ppublish English Journal Article Review

Energy, Life, and ATP (Nobel Lecture).

Angewandte Chemie (International ed. in English) ·Vol. 37 ·No. 17 ·1998-09-18 ·Pages 2296-2307

Boyer PD

Abstract

The puzzling results of 18 O-exchange experiments churned in Paul Boyer's mind, and he realized that the proton-motive force generated upon oxidative phosphorylation is not used primarily for the synthesis of an ATP molecule, but instead its release. The concept of the binding change mechanism was born. For the formation of ATP from ADP and inorganic phosphate-one of the most important reactions in nature-catalysis by ATP synthase requires sequential conformational changes and a rotary mechanism that drives these changes; this enzyme is truly a remarkable molecular machine.

Keywords
ATP Bioenergetics Enzyme catalysis Nobel lecture Phosphorylations
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Boyer Paul D
Department of Chemistry and Biochemistry, University of California at Los Angeles, 611 Circle Drive East, Los Angeles, CA 90095-1570 (USA), Fax: (+1) 310-206-7286.
Article Info
Journal
Angewandte Chemie (International ed. in English)
Abbr.
Angew Chem Int Ed Engl
ISSN
1521-3773
Published
1998-09-18
Pages
2296-2307
Language
English
Region
Germany
NLM ID
0370543
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