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.
Doi
Issei
I
Laboratory of Organic Chemistry, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
Kuse
Masaki
M
Nishikawa
Toshio
T
Isobe
Minoru
M
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