Slow Solvation Dynamics at the Active Site of an Enzyme: Implications for Catalysis
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Slow Solvation Dynamics at the Active Site of an Enzyme: Implications for
Catalysis
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| Creator |
Guha, Soumi
Sahu, Kalyanasis Roy, Durba Mondal, Sudip Kumar Roy, Siddhartha Bhattacharyya, Kankan |
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| Subject |
Structural Biology & Bioinformatics
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| Description |
Solvation dynamics at the active site of an enzyme, glutaminyl-tRNA synthetase (GlnRS),
was studied using a fluorescence probe, acrylodan, site-specifically attached at cysteine residue C229,
near the active site. The picosecond time-dependent fluorescence Stokes shift indicates slow solvation
dynamics at the active site of the enzyme, in the absence of any substrate. The solvation dynamics becomes
still slower when the substrate (glutamine or tRNAGln) binds to the enzyme. A mutant Y211H-GlnRS
was constructed in which the glutamine binding site is disrupted. The mutant Y211H-GlnRS labeled at
C229 with acrylodan exhibited significantly different solvent relaxation, thus demonstrating that the slow
dynamics is indeed associated with the active site. Implications for catalysis and specificity have been
discussed.
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| Publisher |
American Chemical Society
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| Date |
2005
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/364/1/BIOCHEMISTRY_44(_25)__8940%2D8947;2005[51].pdf
Guha, Soumi and Sahu, Kalyanasis and Roy, Durba and Mondal, Sudip Kumar and Roy, Siddhartha and Bhattacharyya, Kankan (2005) Slow Solvation Dynamics at the Active Site of an Enzyme: Implications for Catalysis. Biochemistry, 44. pp. 8940-8947. |
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| Relation |
http://dx.doi.org/10.1021/bi0473915 CCC: $30.25
http://www.eprints.iicb.res.in/364/ |
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