Static and Dynamic Quenching of Tryptophan Fluorescence in Various Proteins by a Chromium (III) Complex
作者： Heather F. Crouse , Elyse M. Petrunak , Ashley M. Donovan , Anna C. Merkle , Brandi L. Swartz
DOI: 10.1080/00387010.2010.546470
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摘要: ABSTRACT The interaction of a chromium (III) complex, (R,R)-N,N′-Bis(3,5-di-tert-butylsalicylidene)-1,2-cyclohexane-diaminochromium (III), with human serum albumin, bovine lysozyme, and free tryptophan was studied using steady-state fluorescence spectroscopy. Dynamic static quenching constants were calculated Stern-Volmer kinetics. complex bound more tightly to the albumins than lysozyme or tryptophan, but only one binding site determined in all systems. also be thermodynamically favorable, on order 103–106. nature Forster distances 1.8–2.0 nm range.
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