Phosphines as a new structural probe of hemoglobin. 1H-NMR evidence for perturbations in the beta heme pocket induced by a thiol reagent.

Abstract

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… (More)

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@article{Bondon1987PhosphinesAA, title={Phosphines as a new structural probe of hemoglobin. 1H-NMR evidence for perturbations in the beta heme pocket induced by a thiol reagent.}, author={Arnaud Bondon and Pasquale Sodano and G{\'e}rard Simonneaux and Constantin T. Craescu}, journal={Biochimica et biophysica acta}, year={1987}, volume={914 3}, pages={289-93} }