Abstract
This chapter presents an experimental work to elucidate how various components of the F 0 F 1 - adenosine triphosphatase (ATPase) system function and interact to carry out and regulate adenosine triphosphate (ATP) synthesis. The chapter discusses the reaction mechanism of F 1 as disclosed by studies with the uncoupler-reversible inhibition of the enzyme by bathophenanthroline-metal chelates. The interaction of F 0 and F 1 based on resolution-reconstitution experiments and the studies of the structure and function of oligomycin sensitivity-conferring protein (OSCP) are presented. The regulation of ATP hydrolysis and ATP synthesis by means of the ATPase-inhibitor (AI) protein, with special reference to the effects of Ca 2 + and Mn 2 + are discussed. The chapter presents attempts to establish which amino acids are destroyed by photooxidation in the presence of Rose Bengal and protected by BPh 3 F 2+ . The derivatives of BPh, which contain a covalent photoaffinity label, such as azide groups attached to the phenyl groups of BPh are prepared and the amino acid residue, which binds the inhibitory chelate, are determined.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
