The detection of mercury, lead, and methylmercury binding sites on lysozyme by carbon-13 NMR chemical shifts of the carboxylate groups.
The chemical shift changes observed in the carbon-13 NMR spectra of the carboxylate region in conjunction with previous fluorescence data indicate that mercury and lead bind to both disulfide bridge 64-80 and to Asp-52 in hen egg-white lysozyme. Methylmercury appears to bind primarily to the disulfide linkage. The carbon-13 NMR results support previous investigations by halide ion NMR and x-ray crystallography. The combined information from all of these techniques is useful for providing a clearer description of heavy metal binding to proteins.
Pesek
J J
JJ
Department of Chemistry, San Jose State University, CA 95192.
Schneider
J F
JF
D001665:Binding Sites; D002247:Carbon Isotopes; D004220:Disulfides; D007854:Lead / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008628:Mercury / Q000378:metabolism*; D008767:Methylmercury Compounds / Q000378:metabolism*; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding
D002247:Carbon Isotopes; D004220:Disulfides; D008767:Methylmercury Compounds; D007854:Lead; D009113:Muramidase; D008628:Mercury