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Static quenching of tryptophan fluorescence in proteins by a dioxomolybdenum(VI) thiolate complex

Paper ID Volume ID Publish Year Pages File Format Full-Text
25889 43907 2014 7 PDF Available
Title
Static quenching of tryptophan fluorescence in proteins by a dioxomolybdenum(VI) thiolate complex
Abstract

•Fluorescence quenching of proteins and tryptophan.•Non-aromatic cis-dioxobis(dithiocarbamato) molybdenum(VI) complex.•Static quenching via H-bond and other forces.•Non-fluorescence complex formation that is exothermic with a negative entropy change.•Binding constants on the order of 104–105 M−1.

The binding of cis-dioxobis(dithiocarbamato) molybdenum(VI) with the proteins bovine serum albumin, human serum albumin, lysozyme, and free tryptophan was studied using fluorescence spectroscopy and Stern–Volmer kinetics. The quenching of tryptophan fluorescence was determined to be static with binding constants on the order of 104–105 M−1, and with a binding site number of one. The interaction was studied over a range of temperatures, and the binding was found to be exothermic with a negative change in entropy. Quantum chemical calculations were also conducted to identify optimal spatial contacts and the resulting energetic contributions between the complex and free tryptophan.

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Keywords
Molybdenum complex; Serum albumins; Tryptophan fluorescence; Static quenching
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Static quenching of tryptophan fluorescence in proteins by a dioxomolybdenum(VI) thiolate complex
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 293, 1 November 2014, Pages 81–87
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us