Abstract
A simple gel equilibration method differing from gel filtration was used for the measurement of ATP binding by purified nitrogenase components from Clostridium pasteurianum. It was clearly established that the binding site in on the iron protein of nitrogenase (Fe protein). Mg 2+ is required for the binding. The Fe protein also binds MgADP. The number of binding sites and the dissociation constants of the MgATP- and MgADP-Fe protein complexes were measured. Inhibition studies indicate that MgADP inhibits MgATP binding by occupying one of the two MgATP sites; MgADP appears to increase slightly the binding of MgATP at its second site.
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.
