title: Porphyrinmaleimides: towards thiol probes for cysteine residues in proteins.
abstract: Porphyrinmaleimides were synthesized and characterized. The thiol-containing amino acid L-cysteine reacted with 58% yield with these porphyrins to form bioconjugate adducts. The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR).
authors: Columbia University, Department of Chemistry, New York, New York 10027, USA.
authors: Yihui
authors: Y
authors: Chen
authors: Timothy
authors: T
authors: Parr
authors: Andrea E
authors: AE
authors: Holmes
authors: Koji
authors: K
authors: Nakanishi
mesh_terms: D003545:Cysteine / Q000032:analysis* / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D008301:Maleimides / Q000138:chemical synthesis* / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry*; D012243:Rhodopsin / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D014466:Ultraviolet Rays
chemical_list: D008301:Maleimides; D011166:Porphyrins; D013438:Sulfhydryl Compounds; C043592:maleimide; D012243:Rhodopsin; D003545:Cysteine