Redox potential tuning through differential quinone binding in the photosynthetic reaction center of Rhodobacter sphaeroides.

ABSTRACT: Ubiquinone forms an integral part of the electron transport chain in cellular respiration and photosynthesis across a vast number of organisms. Prior experimental results have shown that the photosynthetic reaction center (RC) from Rhodobacter sphaeroides is only fully functional with a limited set of methoxy-bearing quinones, suggesting that specific interactions with this substituent are required to drive electron transport and the formation of quinol. The nature of these interactions has yet to be determined. Through parameterization of a CHARMM-compatible quinone force field and subsequent molecular dynamics simulations of the quinone-bound RC, we have investigated and characterized the interactions of the protein with the quinones in the Q(A) and Q(B) sites using both equilibrium simu

SUBMITTER: Vermaas JV 

PROVIDER: S-EPMC4925149 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature