skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Energy capture and use in plants and bacteria. Final technical report

Abstract

The project has centered on elucidation of the mechanism of ATP synthase. The metabolic importance of ATP and the complexity of the ATP synthase have made the problem particularly important and challenging. The development of the binding change mechanism depended upon our recognition of features that were novel in bioenergetics and indeed to the field of enzymology. One important feature of mechanism is that the principal way that energy input from transmembrane proton movement is coupled to ATP formation is to drive conformational changes that cause the release of ATP readily formed and tightly bound at a catalytic site. Another is that three equivalent catalytic sites on the enzyme show strong catalytic cooperativity as they proceed sequentially through different conformations. A more speculative features is that this cooperativity and energy coupling involve a rotational movement of minor subunits relative to the catalytic subunits. During this period these studies have extended and clarified aspects of the synthase mechanism. During assessments of interactions of Mg{sup 2+} and ADP with the synthase we recognized unexpectedly that whether ADP and P{sub i}, or their complexes with Mg{sup 2+} served as substrates for ATP formation by photophosphorylation was not known. Our studies showed that MgADPmore » and free P{sub i} act as substrates.« less

Authors:
Publication Date:
Research Org.:
California Univ., Los Angeles, CA (United States)
Sponsoring Org.:
USDOE, Washington, DC (United States)
OSTI Identifier:
10163235
Report Number(s):
DOE/ER/13845-T3
ON: DE94014592; BR: KC0600000
DOE Contract Number:  
FG03-88ER13845
Resource Type:
Technical Report
Resource Relation:
Other Information: PBD: [1993]
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 14 SOLAR ENERGY; PHOSPHOTRANSFERASES; BIOCHEMICAL REACTION KINETICS; ATP-ASE; ATP; PHOTOSYNTHESIS; OXYGEN 18; MAGNESIUM; PROGRESS REPORT; 550200; 140505; BIOCHEMISTRY; PHOTOCHEMICAL, PHOTOBIOLOGICAL, AND THERMOCHEMICAL CONVERSION

Citation Formats

Boyer, P.D.. Energy capture and use in plants and bacteria. Final technical report. United States: N. p., 1993. Web. doi:10.2172/10163235.
Boyer, P.D.. Energy capture and use in plants and bacteria. Final technical report. United States. doi:10.2172/10163235.
Boyer, P.D.. Fri . "Energy capture and use in plants and bacteria. Final technical report". United States. doi:10.2172/10163235. https://www.osti.gov/servlets/purl/10163235.
@article{osti_10163235,
title = {Energy capture and use in plants and bacteria. Final technical report},
author = {Boyer, P.D.},
abstractNote = {The project has centered on elucidation of the mechanism of ATP synthase. The metabolic importance of ATP and the complexity of the ATP synthase have made the problem particularly important and challenging. The development of the binding change mechanism depended upon our recognition of features that were novel in bioenergetics and indeed to the field of enzymology. One important feature of mechanism is that the principal way that energy input from transmembrane proton movement is coupled to ATP formation is to drive conformational changes that cause the release of ATP readily formed and tightly bound at a catalytic site. Another is that three equivalent catalytic sites on the enzyme show strong catalytic cooperativity as they proceed sequentially through different conformations. A more speculative features is that this cooperativity and energy coupling involve a rotational movement of minor subunits relative to the catalytic subunits. During this period these studies have extended and clarified aspects of the synthase mechanism. During assessments of interactions of Mg{sup 2+} and ADP with the synthase we recognized unexpectedly that whether ADP and P{sub i}, or their complexes with Mg{sup 2+} served as substrates for ATP formation by photophosphorylation was not known. Our studies showed that MgADP and free P{sub i} act as substrates.},
doi = {10.2172/10163235},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Fri Dec 31 00:00:00 EST 1993},
month = {Fri Dec 31 00:00:00 EST 1993}
}

Technical Report:

Save / Share: