化学
色氨酸
猝灭(荧光)
溶菌酶
荧光
动力学
结合常数
牛血清白蛋白
铬
荧光光谱法
环己烷
结合位点
结晶学
色谱法
生物化学
有机化学
氨基酸
物理
量子力学
作者
H. Crouse,Elyse M. Petrunak,Ashley Donovan,A.C. Merkle,Brandi L. Swartz,Swarna Basu
标识
DOI:10.1080/00387010.2010.546470
摘要
ABSTRACT 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 serum albumin, lysozyme, and free tryptophan was studied using steady-state fluorescence spectroscopy. Dynamic and static quenching constants were calculated using Stern-Volmer kinetics. The complex bound more tightly to the serum albumins than to lysozyme or free tryptophan, but only one binding site was determined in all systems. The interaction was also determined to be thermodynamically favorable, and the binding constants were on the order of 103–106. The fluorescence quenching was static in nature with Forster distances in the 1.8–2.0 nm range. KEYWORDS: Cr (III) complexfluorescencestatic and dynamic quenchingStern-Volmertryptophan ACKNOWLEDGMENTS The authors thank Susquehanna University for financial support for this project. They also thank the Chemistry Department at Bryn Mawr College for supporting the initial part of the project.
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