Document Detail


Investigation of Formate Transport through the Substrate Channel of Formate Dehydrogenase by Steered Molecular Dynamics Simulations.
MedLine Citation:
PMID:  21568849     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Steered molecular dynamics simulation has revealed the mechanism of formate transport via the substrate channel of formate dehydrogenase. It is shown that the structural organization of the channel promotes the transport of formate anion in spite of the fact that the channel is too narrow even for such a small molecule. The conformational mobility of Arg284 residue, one of the residues forming the wall of the substrate channel, provides for the binding and delivery of formate to the active site.
Authors:
D K Nilov; I G Shabalin; V O Popov; V K Svedas
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemistry. Biokhimii͡a     Volume:  76     ISSN:  1608-3040     ISO Abbreviation:  Biochemistry Mosc.     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-05-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0376536     Medline TA:  Biochemistry (Mosc)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  172-4     Citation Subset:  IM    
Affiliation:
Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, 119991, Russia. vytas@belozersky.msu.ru.
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