Analysis of all-optical light modulation in proteorhodopsin protein molecules

Abstract

We present a detailed steady-state and time-dependent theoretical analysis of all-optical light modulation in the recently discovered, wild-type proteorhodopsin (WTpR) protein molecules based on excited-state absorption. Amplitude modulation of cw probe laser beam transmissions at 520, 405, 555 and 560 nm, corresponding to the peak absorption of pR, pR M, pR K and pR N intermediate states of pR photocycle, respectively, by cw and pulsed modulating pump laser beam at 520 nm have been analyzed. The effect of various spectral and kinetic parameters on modulation characteristics has been studied. There is an optimum value of concentration for a given pump intensity value for which maximum modulation of the probe beam can be achieved. The switching characteristics of probe beam at 405 and 520 nm exhibit dip and peak, respectively, which can be removed by decreasing the absorption of pR M state at 520 nm. The modulation in WTpR is at lower pump powers with smaller contrast in comparison to WT bacteriorhodopsin (bR) and WT pharaonis phoborhodopsin ( ppR). The modulation characteristics exhibit unique features compared to bR and ppR.