Document Detail

Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin.
MedLine Citation:
PMID:  20643048     Owner:  NLM     Status:  MEDLINE    
In this report, we demonstrate that the internal disulfide bridge in human neuroglobin modulates structural changes associated with ligand photo-dissociation from the heme active site. This is evident from time-resolved photothermal studies of CO photo-dissociation, which reveal a 13.4+/-0.9 mL mol(-1) volume expansion upon ligand photo-release from human neuroglobin, whereas the CO dissociation from rat neuroglobin leads to a significantly smaller volume change (DeltaV=4.6+/-0.3 mL mol(-1)). Reduction of the internal disulfide bond in human neuroglobin leads to conformational changes (reflected by DeltaV) nearly identical to those observed for rat Ngb. Our data favor the hypothesis that the disulfide bond between Cys46 and Cys55 modulates the functioning of human neuroglobin.
Luisana Astudillo; Sophie Bernad; Valérie Derrien; Pierre Sebban; Jaroslava Miksovska
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Publication Detail:
Type:  Letter    
Journal Detail:
Title:  Biophysical journal     Volume:  99     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-20     Completed Date:  2010-10-27     Revised Date:  2011-08-01    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  L16-8     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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MeSH Terms
Carbon Monoxide / chemistry
Disulfides / metabolism*
Globins / chemistry*,  metabolism*
Nerve Tissue Proteins / chemistry*,  metabolism*
Protein Conformation
Spectrum Analysis
Reg. No./Substance:
0/Disulfides; 0/Nerve Tissue Proteins; 0/neuroglobin; 630-08-0/Carbon Monoxide; 9004-22-2/Globins

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