Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 63, Issue 3, Pages 532-535Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2005.05.040
Keywords
human serum albumm; m-nitrophenylfluorone-Mo(VI) complex; fluorescence quenching; energy transfer; binding constant; probe
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In this paper, the binding characteristics of human serum albumin (HSA) and m-nitrophenylfluorone (m-NPF)-molybdenum (MO(VI)) complex have been studied by fluorophotometry. The binding constants are measured at different temperature, Based on the theory of Forster energy transfer, the binding distance and the energy transfer efficiency between m-nitrophenylfluorone-Mo(VI) complex and protein are obtained. According to the thermodynamic parameters, the main sort of binding force can be judged, The results indicate that HSA and m-NPF-Mo(VI) complex have strong interactions. The mechanism of quenching belongs to static quenching and the main sort of binding force is electrostatic gravitation. (c) 2005 Elsevier B.V. All rights reserved.
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