Premium
Energy, Life, and ATP (Nobel Lecture)
Author(s) -
Boyer Paul D.
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19980918)37:17<2296::aid-anie2296>3.0.co;2-w
Subject(s) - energy metabolism , psychology , medicine
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.