scholarly journals Hydrogen Tunneling Links Protein Dynamics to Enzyme Catalysis

2013 ◽  
Vol 82 (1) ◽  
pp. 471-496 ◽  
Author(s):  
Judith P. Klinman ◽  
Amnon Kohen
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis ◽  
Hydrogen Tunneling

Protein dynamics and enzyme catalysis: Insights from simulations

2011 ◽  
Vol 1814 (8) ◽  
pp. 1077-1092 ◽  
Author(s):  
John D. McGeagh ◽  
Kara E. Ranaghan ◽  
Adrian J. Mulholland
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis

Nano-second protein dynamics of key residue at Position 38 in catechol-O-methyltransferase system: a time-resolved fluorescence study

2020 ◽  
Vol 168 (4) ◽  
pp. 417-425
Author(s):  
Fan Liu ◽  
Jianyu Zhang
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis ◽  
Time Resolved Fluorescence ◽  
Fluorescence Study ◽  
Time Resolved ◽  
System A ◽  
Key Enzyme ◽  
Relationship Of ◽  
The Relationship ◽  
Stokes Shifts

Abstract Human catechol-O-methyltransferase, a key enzyme related to neurotransmitter metabolism, catalyses a methyl transfer from S-adenosylmethionine to catechol. Although extensive studies aim to understand the enzyme mechanisms, the connection of protein dynamics and enzyme catalysis is still not clear. Here, W38in (Trp143Phe) and W38in/Y68A (Trp143Phe with Tyr68Ala) mutants were carried out to study the relationship of dynamics and catalysis in nano-second timescale using time-resolved fluorescence lifetimes and Stokes shifts in various solvents. The comprehensive data implied the mutant W38in/Y68A with lower activity is more rigid than the ‘WT’−W38in, suggesting the importance of flexibility at residue 38 to maintain the optimal catalysis.

Preorganization and protein dynamics in enzyme catalysis

2002 ◽  
Vol 2 (1) ◽  
pp. 24-36 ◽  
Author(s):  
P. T. Ravi Rajagopalan ◽  
Stephen J. Benkovic
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis

Protein dynamics and enzyme catalysis: the ghost in the machine?

2012 ◽  
Vol 40 (3) ◽  
pp. 515-521 ◽  
Author(s):  
David R. Glowacki ◽  
Jeremy N. Harvey ◽  
Adrian J. Mulholland
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis ◽  
Isotope Effects ◽  
State Theory ◽  
Quantum Tunnelling ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Kinetic Isotope ◽  
Temperature Dependences ◽  
Multiple Conformations

One of the most controversial questions in enzymology today is whether protein dynamics are significant in enzyme catalysis. A particular issue in these debates is the unusual temperature-dependence of some kinetic isotope effects for enzyme-catalysed reactions. In the present paper, we review our recent model [Glowacki, Harvey and Mulholland (2012) Nat. Chem. 4, 169–176] that is capable of reproducing intriguing temperature-dependences of enzyme reactions involving significant quantum tunnelling. This model relies on treating multiple conformations of the enzyme–substrate complex. The results show that direct ‘driving’ motions of proteins are not necessary to explain experimental observations, and show that enzyme reactivity can be understood and accounted for in the framework of transition state theory.

Linking Protein Dynamics to Enzyme Catalysis

2020 ◽  
pp. 578-588
Author(s):  
Ioanna Zoi ◽  
Dimitri Antoniou ◽  
Steven D. Schwartz
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis
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