7-days of FREE Audio papers, translation & more with Prime
7-days of FREE Prime access
7-days of FREE Audio papers, translation & more with Prime
7-days of FREE Prime access
https://doi.org/10.1016/0926-6577(64)90210-4
Copy DOIJournal: Biochimica et biophysica acta | Publication Date: May 1, 1964 |
Citations: 12 |
Abstract Respiratory activity of chromatophores of Rhodospirillum rubrum, as measured by the O2 uptake, was almost doubled by illumination. Succinoxidase activity of chromatophores was inhibited considerably by o-phenanthroline but not inhibited by KCN either in the dark or light. The aerobic oxidation of p-phenylenediamine in the dark was not inhibited by o-phenanthroline but was completely inhibited by KCN, whereas the oxidation in the light was sensitive to o-phenanthroline but insensitive to KCN. o-Phenanthroline also inhibited other CN−-insensitive reactions in chromatophores, such as photooxidation of reduced cytochrome c2 and the dark-anaerobic oxidation of NADH coupled to the reduction of fumarate. Antimycin A did not inhibit the succinoxidase activity in the dark, but significantly inhibited the activity in the light. Succinate-cytochrome c2 reductase activity was sensitive to antimycin A but insensitive to o-phenanthroline, whereas NADH-cytochrome c2 reductase activity was insensitive to antimycin A but sensitive to o-phenanthroline. The terminal oxidation system in chromatophores is discussed with particular reference to the marked stimulation of O2 uptake by illumination.
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: 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.