Phosphines as a new structural probe of hemoglobin. 1H-NMR evidence for perturbations in the beta heme pocket induced by a thiol reagent.
Binding of trimethylphosphine to myoglobins and hemoglobins from a variety of sources has been examined by 1H-nuclear magnetic resonance. The hemoglobins exhibit two resonances at high field (approx. -3.5 ppm) which have been assigned to PMe3 bound to alpha or to beta subunits. Perturbations in the beta heme pocket induced by a thiol reagent have been detected both in 1H and 31P spectra.
D000818:Animals; D005033:Ethylmaleimide / Q000494:pharmacology*; D006418:Heme / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006859:Hydrogen; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009211:Myoglobin / Q000378:metabolism*; D010720:Phosphines / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity
D006454:Hemoglobins; D046911:Macromolecular Substances; D009211:Myoglobin; D010720:Phosphines; D006418:Heme; C049750:trimethyl phosphine; D006859:Hydrogen; D005033:Ethylmaleimide