Document Detail

Analysis of the iron-sulfur cluster of aconitase by natural and magnetic circular dichroism.
MedLine Citation:
PMID:  7470486     Owner:  NLM     Status:  MEDLINE    
We have examined the iron-sulfur cluster of aconitase, a high-potential iron-sulfur protein, by absorption, circular dichroism (CD), and magnetic circular dichroism (MCD) spectroscopy. The MCD spectrum of unactivated aconitase, which is presumably oxidized, is similar to those of reduced two iron-two sulfide ferredoxins but distinct from the MCD of known four iron-four sulfide proteins. The magnitude of the natural CD of unactivated aconitase also suggests the absence of four iron-four sulfur clusters. Reduction of the enzyme with dithionite and activation with the cysteine-ascorbate-ferrous ion activation mixture generate spectra which are significantly different from those of any iron-sulfur protein seen to date. We interpret these results as indicating that aconitase does not contain a four iron-four sulfur cluster generally thought to be characteristic of high-potential iron-sulfur proteins. It could contain a two iron-two sulfur center or some other center such as a cyclic three iron-three sulfur center.
D Piszkiewicz; O Gawron; J C Sutherland
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  20     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1981 Jan 
Date Detail:
Created Date:  1981-05-13     Completed Date:  1981-05-13     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  363-6     Citation Subset:  IM    
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MeSH Terms
Aconitate Hydratase*
Circular Dichroism
Iron / analysis*
Iron-Sulfur Proteins*
Myocardium / enzymology
Protein Binding
Protein Conformation
Sulfur / analysis*
Grant Support
Reg. No./Substance:
0/Iron-Sulfur Proteins; 0/Metalloproteins; 14844-07-6/Dithionite; 7439-89-6/Iron; 7704-34-9/Sulfur; EC Hydratase

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