Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores.

ABSTRACT: The structural organization of natural pigment-protein complexes provides a specific environment for the chromophore groups. Yet, proteins are inherently dynamic and conformationally mobile. In this work, we demonstrate the heterogeneity of chromophores of C-phycocyanin (C-PC) from Arthrospira platensis. Part of the population of trimeric C-PC is subject to spontaneous disturbances of protein-protein interactions resulting in increased conformational mobility of the chromophores. Upon fluorescence excitation in the visible range, the spectral signatures of these poorly populated states are masked by bulk chromophore states, but the former could be clearly discriminated when the fluorescence is excited by near-infrared quanta. Such selective excitation of conformationally mobile C-PC

SUBMITTER: Tsoraev GV 

PROVIDER: S-EPMC9440762 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature