Organotin-Protein Interactions. Binding of Triethyltin Bromide to Cat Haemoglobin
Document Type
Article
Publication Date
1-1986
Publisher
Portland Press Limited
Source Publication
Biochemical Journal
Source ISSN
0264-6021
Original Item ID
DOI: 10.1042/bj2330471
Abstract
Triethyltin binds to native cat and rat haemoglobin but not to their denatured forms or to other animal haemoglobins. Two molecules of the organotin bind to one molecule of R-state cat haemoglobin with affinity constants of about 1 × 105 M-1. Little or no triethyltin is bound to the deoxygenated (T-state) protein. Binding appears to be dependent upon the existence of a specific three-dimensional configuration of cysteine and histidine residues. The properties of the triethyltin-cat haemoglobin complex are consistent with those of a haemoglobin conformer whose allosteric equilibrium is displaced toward the R-state. Its oxygen affinity and rate of oxidation by nitrite is increased, and the rate of reduction of the methaemoglobin derivative by ascorbate is decreased. These effects of triethyltin are opposite and antagonistic to the effects of inositol hexaphosphate. They are exerted on the alpha- as well as beta-haem groups, even though triethyltin is bound at sites on alpha-globin far removed from the haem groups.
Recommended Citation
Siebenlist, Kevin R. and Taketa, Fumito, "Organotin-Protein Interactions. Binding of Triethyltin Bromide to Cat Haemoglobin" (1986). Biomedical Sciences Faculty Research and Publications. 222.
https://epublications.marquette.edu/biomedsci_fac/222
Comments
Biochemical Journal. Vol. 233, No. 2 (January 1986): 471-477. DOI.