LOV-like flavin-Cys adduct formation by introducing a Cys residue in the BLUF domain of TePixD.
BLUF and LOV are blue-light sensor domains that possess flavin as a common chromophore but exhibit distinct photoreactions. Ile66 located in the BLUF domain of a cyanobacterial photosensor protein, TePixD, was replaced with Cys to mimic the LOV domain. Light-induced Fourier transform infrared spectra of the I66C TePixD showed that a flavin-Cys adduct, typical of the photoinduced intermediates of LOV domains, was formed in the I66C BLUF domain. This result demonstrates that different types of flavin photoreactions can be realized in the same domain if key amino acids are properly arranged near the flavin and the domain structure itself is not a crucial factor to determine the photoreaction type.
Suzuki
Hiroyuki
H
Institute of Materials Science, University of Tsukuba, Tsukuba, Ibaraki 305-8573, Japan.
Okajima
Koji
K
Ikeuchi
Masahiko
M
Noguchi
Takumi
T
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000737:chemistry / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism; D005415:Flavins / Q000737:chemistry* / Q000378:metabolism; D010777:Photochemistry; D020283:Photoreceptors, Microbial / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared
D001426:Bacterial Proteins; D005415:Flavins; D020283:Photoreceptors, Microbial; D003545:Cysteine