Structural Model for the Trialkyltin Binding Site on Cat Hemoglobin |
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Authors: | Ansel L. Chu Fumito Taketa A. Grant Mauk Gary D. Brayer |
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Affiliation: | 1. Department of Biochemistry , University of British Columbia , Vancouver , British Columbia , V6T 1W5 , Canada;2. Department of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin , 53226 |
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Abstract: | Abstract The binding site for trialkyltin complexes on the alpha- chain of cat oxyhemoglobins is proposed to involve the SG and NE2 atoms of Cys-13 and His-113 respectively. On deoxygenation, the conformation of this region changes substantially, allowing complexation only through the ND1 nitrogen atom of His-113, a much less favorable interaction. Thus the model presented explains the preferential binding of trialkyltin complexes to R-state cat hemoglobin and suggests the type of interaction that is likely to occur between these compounds and a variety of less well-characterized enzymes to produce the metabolic effects that trialkyltin complexes are known to produce in vivo. |
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