Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix.

ABSTRACT: The orange carotenoid protein (OCP) is a structurally and functionally modular photoactive protein involved in cyanobacterial photoprotection. Recently, based on bioinformatic analysis and phylogenetic relationships, new families of OCP have been described, OCP2 and OCPx. The first characterization of the OCP2 showed both faster photoconversion and back-conversion, and lower fluorescence quenching of phycobilisomes relative to the well-characterized OCP1. Moreover, OCP2 is not regulated by the fluorescence recovery protein (FRP). In this work, we present a comprehensive study combining ultrafast spectroscopy and structural analysis to compare the photoactivation mechanisms of OCP1 and OCP2 from Tolypothrix PCC 7601. We show that despite significant differences in their functional character

SUBMITTER: Kuznetsova V 

PROVIDER: S-EPMC6943196 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature