Document Detail


Cytochrome c and SDS: a molten globule protein with altered axial ligation.
MedLine Citation:
PMID:  14757060     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Saccharomices cerevisiae (yeast iso-1) cytochrome c has been investigated in the presence of 100 mM SDS in order to simulate the interaction of cytochrome c with membrane. Under these circumstances, a high spin species with detached methionine axial ligand is observed through NMR, in analogy to findings on the horse heart protein. However, at variance with the latter system, for the yeast protein also a low spin species is detected, which appears to be present with a concentration of about 40% with respect to that of the high spin species. The R(1), R(2), [1H]-15N NOE of backbone amides which are not affected by paramagnetism are homogeneous and allow a simultaneous analysis of the data for the two species. The result is that the rotational correlation time is larger than in water and larger than expected on the basis of viscosity of the SDS-containing solution. This finding suggests interactions of cytochrome c with SDS. Furthermore, it appears that there is subnanosecond backbone mobility, which also accounts for the decreased intensity of NOE cross-peaks and may be associated with equilibria between helical and random coil structure. The dynamic behavior appears to be a common feature of the high spin and low spin species and is consistent with the presence of a molten globule state. The molten globule nature of the protein could account for the presence of the different axial coordination of the heme iron. Such findings are meaningful with respect to the physiology of cytochrome c as electron transfer protein and as promoter of apoptosis.
Authors:
Ivano Bertini; Paola Turano; Paul R Vasos; Arnaud Bondon; Soizic Chevance; Gérard Simonneaux
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  336     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2004 Feb 
Date Detail:
Created Date:  2004-02-03     Completed Date:  2004-03-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  489-96     Citation Subset:  IM    
Affiliation:
CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy. bertini@cerm.unifi.it
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MeSH Terms
Descriptor/Qualifier:
Animals
Cytochromes c / chemistry*
Horses
Magnetic Resonance Spectroscopy
Myocardium / chemistry
Protein Conformation
Protons
Rotation
Saccharomyces cerevisiae / chemistry
Saccharomyces cerevisiae Proteins / chemistry
Sodium Dodecyl Sulfate / chemistry*
Time Factors
Viscosity
Chemical
Reg. No./Substance:
0/Protons; 0/Saccharomyces cerevisiae Proteins; 151-21-3/Sodium Dodecyl Sulfate; 9007-43-6/Cytochromes c

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


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