Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 99, Issue 2, Pages 78-86Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2010.02.009
Keywords
Time resolved spectroscopy; Circular dichroism; Rhodamine 6G; Hemoglobin; Static quenching; Hydrophobic interactions
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Funding
- Council of Scientific and Industrial Research (CSIR), New Delhi, India [01 (1883)/03/EMR-II]
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UV-vis, time-resolved fluorescence and circular dichroism spectroscopic investigations have been made to reveal the nature of the interactions between xanthene dye Rhodamine 6G and the well known protein hemoglobin. From the analysis of the steady-state and time-resolved fluorescence quenching of Rhodamine 6G in aqueous solutions in presence of hemoglobin, it is revealed that the quenching is static in nature. The primary binding pattern between Rhodamine and hemoglobin has been interpreted as combined effect of hydrophobic association and electrostatic interaction. The binding constants, number of binding sites and thermodynamic parameters at various pH of the environment have been computed. The binding average distance between the energy donor Rhodamine and acceptor hemoglobin has been determined from the Forster's theory. (C) 2010 Elsevier B.V. All rights reserved.
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