Abstract
Flavocytochrome c-552, isolated from the photosynthetic purple sulfur bacterium Chromatium vinosum, after linkage to an Affigel 10-affinity matrix, will bind equine and yeast mitochondrial cytochromes c, C. vinosum cytochrome c-550 and cytochrome c 2 from the photosynthetic purple non-sulfur bacterium Rhodo-pseudomonas viridis. Similarly, an equine cytochrome c-Sepharose 4B affinity column will bind the C. vinosum flavocytochrome c-552 and its separated heme-containing subunit. These results and the correlation between the effect of ionic strength on binding of the flavocytochrome c-552 to cytochrome c and on the sulfide:cytochrome c oxidoreductase activity catalyzed by C. vinosum flavocytochrome c-552 support the idea of the involvement of an electrostatic complex between the two proteins during sulfide oxidation.
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.
