Cadmium-substituted skeletal troponin C metal binding investigations and sequence assignment of the cadmium-113 resonances.
The binding of cadmium to the calcium binding subunit of skeletal troponin (STnC) has been reinvestigated using direct binding methods and fluorescent derivatives. These data provide straightforward explanations of the observed titration behavior in the 113Cd NMR (Ellis, P.D., Strang, P., and Potter, J.D. (1984) J. Biol. Chem. 259, 10348-10356). Further, fluorescent derivatives of skeletal troponin C provide an excellent means of establishing a sequence assignment for the resonances observed in the 113Cd NMR. The results of these experiments demonstrate that sites I and II, the Ca2+ regulatory sites, can be assigned to resonances at -108.5 and -101.5 ppm, respectively. Sites III and IV, the structural sites, are assigned to resonances -112.8 and -106.8 ppm, respectively. These data are discussed in terms of recent structural findings and speculations.
Ellis
P D
PD
Department of Chemistry, University of South Carolina, Columbia 29208.
Marchetti
P S
PS
Strang
P
P
Potter
J D
JD
D000818:Animals; D001665:Binding Sites; D002104:Cadmium / Q000494:pharmacology*; D002118:Calcium / Q000378:metabolism*; D007554:Isotopes; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009132:Muscles / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014336:Troponin / Q000378:metabolism*; D019209:Troponin C
D007554:Isotopes; D014336:Troponin; D019209:Troponin C; D002104:Cadmium; D002118:Calcium