Metalloselenonein, the selenium analogue of metallothionein: synthesis and characterization of its complex with copper ions.
We used an automated peptide synthesizer to produce a peptide, metalloselenonein, that contains selenocysteine residues substituted for all cysteine residues in Neurospora crassa copper metallothionein. Metalloselenonein binds 3 mol of Cu(I) per mol. This adduct shows a broad absorption band between 230 and 400 nm and a fluorescence band at 395 nm, which can be attributed to copper-selenolate coordination. The circular dichroism spectrum of the copper-metalloselenonein complex shows a positive band around 245 nm attributable to asymmetry in metal coordination.
Oikawa
T
T
Institute for Chemical Research, Kyoto University, Japan.
Esaki
N
N
Tanaka
H
H
Soda
K
K
D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D003545:Cysteine / Q000031:analogs & derivatives* / Q000502:physiology; D008668:Metallothionein / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry*; D009492:Neurospora crassa; D012643:Selenium / Q000502:physiology*; D017279:Selenocysteine; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis; D013329:Structure-Activity Relationship
D000596:Amino Acids; D017279:Selenocysteine; C068269:metalloselenonein; D003300:Copper; D008668:Metallothionein; D012643:Selenium; D003545:Cysteine