Adenosine triphosphate synthase- A unique cellular power generator

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 conforma...

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Bibliographic Details
Main Author: Heralde, Francisco M., III
Format: text
Published: Animo Repository 1998
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Online Access:https://animorepository.dlsu.edu.ph/faculty_research/7692
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Institution: De La Salle University
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Summary: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.