Selective protein modification by the hydroperoxide intermediate in a photoprotein, aequorin.
During the course of protein modification program, we employed a recombinant aequorin, the apo-protein reconstituted with coelenterazine, and found out that the photolytic hyperperoxide modified three -S-SCH2CHOHCHOHCH2SH groups to -S-SCH2CHOHCH=CH-S=O)H or -S-SCH2CHOHCH=CH-S(=O)OH of terminal DTT connected to cysteine residues of the C145, C152 and C180, which turned out to locate near the chromophore.
Laboratory of Organic Chemistry, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
Issei
I
Doi
Masaki
M
Kuse
Toshio
T
Nishikawa
Minoru
M
Isobe
D000331:Aequorin / Q000737:chemistry* / Q000528:radiation effects; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D003545:Cysteine / Q000737:chemistry; D006861:Hydrogen Peroxide / Q000737:chemistry* / Q000528:radiation effects; D037402:Hydrozoa; D049408:Luminescent Agents; D013058:Mass Spectrometry; D008715:Methionine / Q000737:chemistry; D017382:Reactive Oxygen Species / Q000737:chemistry
D000596:Amino Acids; D049408:Luminescent Agents; D017382:Reactive Oxygen Species; D000331:Aequorin; D008715:Methionine; D006861:Hydrogen Peroxide; D003545:Cysteine