Role of active site conformational changes in photocycle activation of the AppA BLUF photoreceptor.

ABSTRACT: Blue light using flavin adenine dinucleotide (BLUF) proteins are essential for the light regulation of a variety of physiologically important processes and serve as a prototype for photoinduced proton-coupled electron transfer (PCET). Free-energy simulations elucidate the active site conformations in the AppA (activation of photopigment and puc expression) BLUF domain before and following photoexcitation. The free-energy profile for interconversion between conformations with either Trp104 or Met106 closer to the flavin, denoted Trp_in/Met_out and Trp_out/Met_in, reveals that both conformations are sampled on the ground state, with the former thermodynamically favorable by ∼3 kcal/mol. These results are consistent with the experimental observat

SUBMITTER: Goyal P 

PROVIDER: S-EPMC5321014 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature