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Steady‐state fluorescence and circular dichroism of trout hemoglobins I and IV interacting with tributyltin
Author(s) -
Zolese G.,
Gabbianelli R.,
Caulini G.C.,
Bertoli E.,
Falcioni G.
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19990301)34:4<443::aid-prot4>3.0.co;2-d
Subject(s) - tributyltin , circular dichroism , trout , fluorescence , chemistry , biophysics , physics , stereochemistry , biology , fish <actinopterygii> , fishery , optics , environmental chemistry
The effect of tributyltin chloride (TBTC) on rainbow trout ( Salmo irideus ) hemoglobin I (HbI) and hemoglobin IV (HbIV) was characterized by the steady‐state fluorescence of intrinsic and extrinsic fluorescent probes. The fluorescence emission spectrum (λ ex 280 nm) is greatly increased in intensity by the presence of the organotin in both proteins. Circular dichroism spectra in the same samples show a small decrease in θ 222 , a measure correlated with the percentage of the α‐helical content. Morever, important changes in near‐UV, Soret, and visible regions of CD were induced by TBTC. The correlation of data obtained with trout hemoglobins (HbI and HbIV) with similar measurements on globins suggests that the presence of heme is necessary for the interaction of the organotin compound with the proteins. Proteins 1999;34:443–452. © 1999 Wiley‐Liss, Inc.