Ultrafast All-Optical Switching Using Doped Chromoprotein Films

Abstract

Next-generation communication networks require > Tbit/s single-channel data transfer and processing with subpicosecond switches and routers at network nodes. Materials enabling ultrafast all-optical switching have high potential to solve the speed limitations of current optoelectronic circuits. Chromoproteins exhibit a large light-controlled refractive index change alleviating the driving energy requirements for optical switching. Here, we report femtosecond transient grating experiments demonstrating the feasibility of < 200 fs all-optical switching by hydrated thin films of photoactive yellow protein and compare the results with those obtained using bacteriorhodopsin. Possibilities for the practical utilization of the scheme in extremely highspeed optical modulation and switching/routing with nominally infinite extinction contrast are discussed.

Photoactive yellow protein adsorption at hydrated polyethyleneimine and poly-L-glutamic acid interfaces

“…A detailed knowledge about these complex phenomena, dominated by electrostatic, van der Waals, and hydrophobic interactions, is also crucial when designing biomaterials for 3 implants, medical devices, and bioelectronics. On the other hand, photosensitive coatings based on biomolecules are attractive due to their biodegradability and easy manufacturability for the conversion of light to electrical energy [16], and for integrated optics [17][18][19]. In such applications, controlled immobilization of proteins is needed to create well-ordered protein layers with high optical quality.…”

Photoactive Yellow Protein Adsorption at Hydrated Polyethyleneimine and Poly-l-Glutamic Acid Interfaces

“…A detailed knowledge about these complex phenomena, dominated by electrostatic, van der Waals, and hydrophobic interactions, is also crucial when designing biomaterials for implants, medical devices, and bioelectronics. On the other hand, photosensitive coatings based on biomolecules are attractive due to their biodegradability and easy manufacturability for the conversion of light to electrical energy [ 16 ], and for integrated optics [ 17 , 18 , 19 ]. In such applications, a controlled immobilization of proteins is needed to create well-ordered protein layers with high optical quality.…”

“…PYP is a hydrophilic, 14 kDa protein consisting of 125 amino acids and its structure often serves as a model for understanding biologically important photoreceptors, such as rhodopsins, and receptor activation in biological signal transduction processes [ 42 , 43 , 44 ]. Recently, PYP received more attention due to its possible application in bioelectronics and integrated optics [ 18 , 19 , 45 , 46 , 47 ]. PYP belongs to the group of globular proteins and is the model structure for the PAS-(Per–Arnt–Sim) domain superfamily, which is a signal transduction α/β pathway structure commonly found in prokaryotic and eukaryotic organisms [ 48 ].…”

Microsecond All-Optical Modulation by Biofunctionalized Porous Silicon Microcavity

“…More recently, dried samples from other chromoproteins, most notably photoactive yellow protein (PYP), have also been proven to possess NLO properties making them suitable for use as NLO materials in future integrated optic applications [ 13 , 14 , 15 , 16 ]. PYP is a 14 kDa water-soluble protein that drives negative phototaxis in purple sulfur bacteria, such as Halorhodospira halophila [ 17 ].…”

“…A row of recent studies present thorough analyses of the unique spectrokinetic properties of PYP films, including their high second-order nonlinearities, responsible for a Kerr-constant (4 × 10 −4 ) that is several orders of magnitude higher than conventional nonlinear-optical signals, and a light-induced refractive index change reaching the 10 −3 magnitude [ 13 , 14 , 15 , 16 ]. Based on these observations, PYP films can be considered promising alternatives to bR-based NLO elements in future integrated optical applications.…”