Triethyltin binding to cat haemoglobin. Evidence for two chemically distinct sites and a role for both histidine and cysteine residues

Triethyltin binding to cat haemoglobin was measured after pretreatment of the protein with diethyl pyrocarbonate at pH 6.0,iodoacetamide or phenylmercuric acetate or by photo-oxidation in the presence of Methylene Blue. The pentaco-ordinate nature of the binding of triethyltin to cat haemoglobin is...

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Bibliographic Details
Published in:Biochemical journal 1979-02, Vol.177 (2), p.461-470
Main Authors: Elliott, B.M, Aldridge, W.N, Bridges, J.W
Format: Article
Language:English
Subjects:
animal science
Animals
Binding Sites
Cats
Chemical Phenomena
Chemistry
Cysteine - metabolism
Diethyl Pyrocarbonate - pharmacology
Hemoglobins - metabolism
Histidine - metabolism
livestock
Models, Chemical
Protein Binding - drug effects
Proteins - metabolism
Trialkyltin Compounds - metabolism
Triethyltin Compounds - metabolism
zoology
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Summary:Triethyltin binding to cat haemoglobin was measured after pretreatment of the protein with diethyl pyrocarbonate at pH 6.0,iodoacetamide or phenylmercuric acetate or by photo-oxidation in the presence of Methylene Blue. The pentaco-ordinate nature of the binding of triethyltin to cat haemoglobin is confirmed by the inability of intramolecularly pentaco-ordinate tin compounds to compete. Consideration of the symmetry of the haemoglobin molecule in the light of the above results suggests that a unique arrangement of histidine and cysteine residues is required for the binding of triethyltin. The effects of treatment with diethyl pyrocarbonate of other preparations which bind triethyltin (rat liver supernatant, a fraction from rat liver mitochondria and rat brain myelin) were determined and shown to be complex.
ISSN:0306-3275
0264-6021
1470-8728
DOI:10.1042/bj1770461