Document Detail

Chloroperoxidase-catalyzed epoxidation of cis-β-methylstyrene: distal pocket flexibility tunes catalytic reactivity.
MedLine Citation:
PMID:  23020548     Owner:  NLM     Status:  MEDLINE    
Chloroperoxidase, the most versatile heme protein, has a hybrid active site pocket that shares structural features with peroxidases and cytochrome P450s. The simulation studies presented here show that the enzyme possesses a remarkable ability to efficiently utilize its hybrid structure, assuming structurally different peroxidase-like and P450-like distal pocket faces and thereby enhancing the inherent catalytic capability of the active center. We find that, during epoxidation of cis-β-methylstyrene (CBMS), the native peroxidase-like aspect of the distal pocket is diminished as the polar Glu183 side chain is displaced away from the active center and the distal pocket takes on a more hydrophobic, P450-like, aspect. The P450-like distal pocket provides a significant enthalpic stabilization of ∼4 kcal/mol of the 14 kcal/mol reaction barrier for gas-phase epoxidation of CMBS by an oxyferryl heme-thiolate species. This stabilization comes from breathing of the distal pocket. As until recently the active site of chloroperoxidase was postulated to be inflexible, these results suggest a new conceptual understanding of the enzyme's versatility: catalytic reactivity is tuned by flexibility of the distal pocket.
Alexander N Morozov; David C Chatfield
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-10-19
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  116     ISSN:  1520-5207     ISO Abbreviation:  J Phys Chem B     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-01     Completed Date:  2013-03-26     Revised Date:  2013-11-06    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  United States    
Other Details:
Languages:  eng     Pagination:  12905-14     Citation Subset:  IM    
Department of Chemistry and Biochemistry, Florida International University, Miami, Florida 33199, United States.
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MeSH Terms
Catalytic Domain*
Chloride Peroxidase / chemistry*,  metabolism*
Enzyme Stability
Epoxy Compounds / chemistry*
Hydrophobic and Hydrophilic Interactions
Molecular Dynamics Simulation*
Quantum Theory
Styrenes / chemistry*
Grant Support
Reg. No./Substance:
0/Epoxy Compounds; 0/Protons; 0/Styrenes; 25013-15-4/vinyltoluene; EC Peroxidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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