How Light-Induced Charge Transfer Accelerates the Receptor-State Recovery of Photoactive Yellow Protein from its Signaling State

Abstract

Stark (electroabsorption) spectra of the M100A mutant of photoactive yellow protein reveal that the neutral, cis cofactor of the pB intermediate undergoes a strikingly large change in the static dipole moment ( | Δ μ → | =19 Debye) on photon absorption. The formation of this charge-separated species, in the excited state, precedes the cis → trans isomerization of the pB cofactor and the regeneration of pG. The large | Δ μ → | , reminiscent of that produced on the excitation of pG, we propose, induces twisting of the cis cofactor as a result of translocation of negative charge, from the hydroxyl oxygen, O1, toward the C7-C8 double bond. The biological significance of this photoinduced charge transfer reaction underlies the significantly faster regeneration of pG from pB in vitro, on the absorption of blue light.