Abstract
Abstract Protein binding properties of fac -rhenium(I) complexes with general structure [Re(CO) 3 (N-N)L]PF 6 , where N-N = 4,4′-dinanoyl-2,2-bipyridine and L = py-3-COOH ( 1a ) and py-3-CONH 2 ( 1b ) with bovine serum albumin (BSA) were investigated at physiological pH (7.4) using UV–visible absorption and fluorescence spectral study, excited state lifetime measurement and circular dichroism (CD). The results observed from fluorescence spectra reveal the energy transfer from BSA to Re(I) complex, and the distance r between donor (BSA) and acceptor (Re(I) complex) is 3.05 nm and 2.16 nm for 1a and 1b respectively according to Forster's non-radiative energy transfer theory. CD results show that the binding of Re(I) complex could induce the conformational change with the loss of α-helicity.
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 callMore From: Journal of Photochemistry and Photobiology A: Chemistry
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.
