Skip navigation
  • Home
  • Browse
    • Communities
      & Collections
    • Browse Items by:
    • Publication Date
    • Author
    • Title
    • Subject
    • Department
  • Sign on to:
    • My MacSphere
    • Receive email
      updates
    • Edit Profile


McMaster University Home Page
  1. MacSphere
  2. Open Access Dissertations and Theses Community
  3. Open Access Dissertations and Theses
Please use this identifier to cite or link to this item: http://hdl.handle.net/11375/6324
Title: Model Studies on Biological Energy Conversion Mechanisms
Authors: Huang, Kun-Po
Advisor: Bader, Richard F. W.
Department: Chemistry
Keywords: Chemistry;Chemistry
Publication Date: Sep-1981
Abstract: <p>This thesis is concerned with the design of ATP-producing physical and chemical model systems and the investigation of the mechanisms of ATP formation at the molecular level. The ultimate purpose of this study is to apply the concepts derived from these model systems to more complex biological systems. The mechanisms of energy transduction in living organisms may then be approached at a molecular level.</p> <p>Based on the study of the model systems, three modes of activation during the ATP-forming chemical steps for either ADP or inorganic phosphate have been identified. They are:</p> <p>(1) Through a one-electron reduction of ADP into a radical form;</p> <p>(2) Through the creation of oxidizing agents with redox potentials sufficient to oxidize inorganic phosphate;</p> <p>(3) Through an activation of phosphate by coordination to a reduced hemecomplex, followed by aerobic oxidation of the resultant phosphate-heme complex.</p> <p>In biological systems, the first mode may involve utilization of a reducing power of an electron transport chain, of a reducing functional group such as thiol in the ATP synthetase. The second mode may involve PS II or generation of delta singlet oxygen by various energy transfer processes. The third mode may involve the coordination of inorganic phosphate to a cytochrome, such as cytochrome-a₃ in an cytochrome-c oxidase complex.</p>
URI: http://hdl.handle.net/11375/6324
Identifier: opendissertations/1642
2051
1239485
Appears in Collections:Open Access Dissertations and Theses

Files in This Item:
File SizeFormat 
fulltext.pdf
Open Access
4.96 MBAdobe PDFView/Open
Show full item record Statistics


Items in MacSphere are protected by copyright, with all rights reserved, unless otherwise indicated.

Sherman Centre for Digital Scholarship     McMaster University Libraries
©2022 McMaster University, 1280 Main Street West, Hamilton, Ontario L8S 4L8 | 905-525-9140 | Contact Us | Terms of Use & Privacy Policy | Feedback

Report Accessibility Issue