Document Detail


Solvent-slaved protein motions accompany proton but not hydride tunneling in light-activated protochlorophyllide oxidoreductase.
MedLine Citation:
PMID:  19373814     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
H(+) but not H(-): The reduction reaction of protochlorophyllide catalyzed by protochlorophyllide oxidoreductase features solvent-slaved motions that control the proton- but not the hydride-tunneling mechanism. These motions imply a long-range dynamic network from the solvent to the enzyme active site that facilitate proton transfer (see picture, left). Motions for hydride transfer are more localized and are not slaved by the solvent (see picture, right).
Authors:
Derren J Heyes; Michiyo Sakuma; Nigel S Scrutton
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Angewandte Chemie (International ed. in English)     Volume:  48     ISSN:  1521-3773     ISO Abbreviation:  Angew. Chem. Int. Ed. Engl.     Publication Date:  2009  
Date Detail:
Created Date:  2009-05-11     Completed Date:  2009-06-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370543     Medline TA:  Angew Chem Int Ed Engl     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  3850-3     Citation Subset:  IM    
Affiliation:
Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK. derren.heyes@manchester.ac.uk
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MeSH Terms
Descriptor/Qualifier:
Cyanobacteria / enzymology
Enzyme Activation / radiation effects
Hydrogen / chemistry*
Light
Molecular Structure
Oxidoreductases Acting on CH-CH Group Donors / metabolism*
Photochemical Processes
Protons*
Solvents / chemistry*
Viscosity
Grant Support
ID/Acronym/Agency:
//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Protons; 0/Solvents; 1333-74-0/Hydrogen; EC 1.3.-/Oxidoreductases Acting on CH-CH Group Donors; EC 1.3.1.33/protochlorophyllide reductase

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


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