Mechanically driven ATP synthesis by F-1-ATPase

Itoh, H., Takahashi, A., Adachi, K., Noji, H., Yasuda, R., Yoshida, M., Kinosita, K. (January 2004) Mechanically driven ATP synthesis by F-1-ATPase. Nature, 427 (6973). pp. 465-468. ISSN 0028-0836

URL: http://www.nature.com/nature/journal/v427/n6973/fu...
DOI: 10.1038/nature02212

Abstract

ATP, the main biological energy currency, is synthesized from ADP and inorganic phosphate by ATP synthase in an energy-requiring reaction(1-3). The F-1 portion of ATP synthase, also known as F-1-ATPase, functions as a rotary molecular motor: in vitro its gamma-subunit rotates(4) against the surrounding alpha(3)beta(3) subunits(5), hydrolysing ATP in three separate catalytic sites on the beta-subunits. It is widely believed that reverse rotation of the gamma-subunit, driven by proton flow through the associated F-o portion of ATP synthase, leads to ATP synthesis in biological systems(1-3,6,7). Here we present direct evidence for the chemical synthesis of ATP driven by mechanical energy. We attached a magnetic bead to the gamma-subunit of isolated F-1 on a glass surface, and rotated the bead using electrical magnets. Rotation in the appropriate direction resulted in the appearance of ATP in the medium as detected by the luciferase-luciferin reaction. This shows that a vectorial force ( torque) working at one particular point on a protein machine can influence a chemical reaction occurring in physically remote catalytic sites, driving the reaction far from equilibrium.

Item Type: Paper
Uncontrolled Keywords: MOLECULAR MOTOR SYNTHASE F1-ATPASE DIMETHYLSULFOXIDE RESOLUTION NUCLEOTIDE ROTATION BINDING ENERGY MYOSIN
Subjects: bioinformatics > genomics and proteomics > small molecules > ATP
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
CSHL Authors:
Depositing User: CSHL Librarian
Date: January 2004
Date Deposited: 03 Feb 2012 15:26
Last Modified: 03 Feb 2012 15:26
URI: http://repository.cshl.edu/id/eprint/22396

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