Abstract
In a previous study on the anaerobic electron transport in the wild-type and a mutant strain of Paracoccus denitrificans, the differences in sensitivity towards the copper-chelating agent diethyldithiocarbamate have been interpreted to arise from a substitution of a soluble copper protein for the absent cytochrome c 550. Here it is shown that two factors complicate this interpretation: (i) diethyldithiocarbamate can also inhibit through interaction with (a) site(s) located in the cytoplasmic membrane and (ii) it has the potential of being a good electron donor for c-type cytochromes. The participation of a copper protein in the denitrification pathway thus needs to be verified by independent means.
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.
