Adenosine triphosphate synthase- A unique cellular power generator

• Main Author: Heralde, Francisco M., III
• Format: text
• Published: Animo Repository 1998
• Subjects: Adenosine triphosphate—Synthesis; Proton exchange membrane fuel cells; Biochemistry, Biophysics, and Structural Biology
• Online Access: https://animorepository.dlsu.edu.ph/faculty_research/7692
• Institution: De La Salle University

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.