Rectified photocurrent in a protein based molecular photo-diode consisting of a cytochrome b562-green fluorescent protein chimera self-assembled monolayer.
We fabricated a self-assembled monolayer (SAM) of a chimeric protein created as a novel model protein for an artificial light-harvesting complex (LHC) composed of two proteins, cytochrome b(562) (cytb(562)) mutated for SAM fabrication (cytb(562), N22C, G82C) and enhanced green fluorescent protein (EGFP). The SAM formation of chimeric protein on a single-crystalline Au(111) substrate was confirmed by atomic force microscopy (AFM) measurement. The rectified photocurrent of the chimeric protein SAM on a gold substrate was detected by light-illumination scanning tunneling microscopy (LI-STM) co-operated with a lock-in technique. The photocurrent generation of the chimeric protein SAM was wavelength-specific to the light-illumination (488 nm), which indicated that the EGFP part of the chimera plays a role as a sensitizer in the photo-induced electron transfer process.
Lee
Bumhwan
B
Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Takeda
Shuji
S
Nakajima
Ken
K
Noh
Jaegeun
J
Choi
Jeongwoo
J
Hara
Masahiko
M
Nagamune
Teruyuki
T
D015374:Biosensing Techniques / Q000295:instrumentation*; D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D008954:Models, Biological; D010788:Photosynthesis / Q000502:physiology; D011993:Recombinant Fusion Proteins; D013053:Spectrophotometry; D013997:Time Factors
D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D011993:Recombinant Fusion Proteins; C017850:cytochrome b562, E coli