[The ability of green fluorescent proteins for photoconversion under oxygen-free conditions is determined by the chromophore structure rather than its amino acid environment].
Photoconversion of various green and cyan fluorescent proteins to the form fluorescing in the red area of the visible spectrum under the oxygen-free conditions was studied. Such photoconversion has earlier been described for the EGFP green fluorescent protein. Phylogenetically distant fluorescent proteins that have a low homology of their amino acid sequences but contain chemically identical chromophores based on a Tyr residue were shown to be susceptible to this type of photoconversion. At the same time, the ECFP protein, which has 92% homology with EGFP but contains a chromophore based on tryptophan did not undergo the photoconversion. Thus, it is precisely the chromophore structure, rather than the amino acid environment that determines the ability of green fluorescent proteins to display photoconversion to the red fluorescent state under anaerobic conditions.
Kiseleva
Iu V
IuV
Mishin
A S
AS
Bogdanov
A M
AM
Labas
Iu A
IuA
Luk'ianov
K A
KA
D000595:Amino Acid Sequence; D000693:Anaerobiosis; D000818:Animals; D037421:Anthozoa; D003063:Cnidaria; D003445:Crustacea; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000528:radiation effects; D008027:Light; D008969:Molecular Sequence Data; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
C527701:enhanced cyan fluorescent protein; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; D014443:Tyrosine; D014364:Tryptophan