Adenosine triphosphate synthase- A unique cellular power generator

Authors

Francisco M. Heralde III

College

College of Science

Department/Unit

Biology

Document Type

Article

Source Title

CvSU Research Journal

Volume

12

Issue

1&2

First Page

66

Last Page

73

Publication Date

1998

Abstract

Major achievements in structural and functional education on the enzyme adenosine triphosphate (ATP) synthase are reported. Ubiquitous occurrence and evolutionary conservation are also demonstrated. The structure and functional relevance of the F₁ portion have been resolved particularly the conformational coupling of catalytic activity which involves the internal rotation of the y-sub-unit in promoting the binding change mechanism. Integration of recent findings on the F₀ portion supports the "proton well" concept. Sub-unit functions are considered in relation to proton translocation and rotational catalysis. Variations in bacterial, mitochondrial and chloroplast forms are presented.

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Recommended Citation

Heralde, F. M. (1998). Adenosine triphosphate synthase- A unique cellular power generator. CvSU Research Journal, 12 (1&2), 66-73. Retrieved from https://animorepository.dlsu.edu.ph/faculty_research/7692

Disciplines

Biochemistry, Biophysics, and Structural Biology

Keywords

Adenosine triphosphate—Synthesis; Proton exchange membrane fuel cells

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