Document Detail

The transient catalytically competent coenzyme allocation into the active site of Anabaena ferredoxin NADP(+)-reductase.
MedLine Citation:
PMID:  21538059     Owner:  NLM     Status:  Publisher    
Ferredoxin-NADP(+) reductase (FNR) catalyses the electron transfer from ferredoxin to NADP(+) via its flavin FAD cofactor. A molecular dynamics theoretical approach is applied here to visualise the transient catalytically competent interaction of Anabaena FNR with its coenzyme, NADP(+). The particular role of some of the residues identified as key in binding and accommodating the 2'P-AMP moiety of the coenzyme is confirmed in molecular terms. Simulations also indicate that the architecture of the active site precisely contributes to the orientation of the N5 of the FAD isoalloxazine ring and the C4 of the coenzyme nicotinamide ring in the conformation of the catalytically competent hydride transfer complex and, therefore, contributes to the efficiency of the process. In particular, the side chain of the C-terminal Y303 in Anabaena FNR appears key to providing the optimum geometry by reducing the stacking probability between the isoalloxazine and nicotinamide rings, thus providing the required co-linearity and distance among the N5 of the flavin cofactor, the C4 of the coenzyme nicotinamide and the hydride that has to be transferred between them. All these factors are highly related to the reaction efficiency, mechanism and reversibility of the process.
José Ramón Peregrina; Isaías Lans; Milagros Medina
Related Documents :
19029339 - The mad2 partial unfolding model: regulating mitosis through mad2 conformational switch...
11864969 - The role of atp hydrolysis for kinesin processivity.
9811789 - Nuclear localization signal receptor importin alpha associates with the cytoskeleton.
6977619 - On the identification of alpha- and beta-tubulin subunits.
18586949 - Glutamylation on alpha-tubulin is not essential but affects the assembly and functions ...
15082749 - Methylphenidate is stereoselectively hydrolyzed by human carboxylesterase ces1a1.
10951189 - Nucleotide-binding domain 1 of cystic fibrosis transmembrane conductance regulator prod...
22677029 - A sar study on a series of synthetic lipophilic chalcones as inhibitor of transcription...
16894479 - Beta-glucosidase catalyzing specific hydrolysis of an iridoid beta-glucoside from plume...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-5-3
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  -     ISSN:  1432-1017     ISO Abbreviation:  -     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-5-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias and Institute of Biocomputation and Physics of Complex Systems (BIFI), Universidad de Zaragoza, 50009, Zaragoza, Spain.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  Structural stability and unfolding transition of ?-glucosidases: a comparative investigation on isoz...
Next Document:  Low-density lipoprotein cholesterol suppresses apoptosis in human multiple myeloma cells.