Document Detail


Analysis of the iron-sulfur cluster of aconitase by natural and magnetic circular dichroism.
MedLine Citation:
PMID:  7470486     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
D Piszkiewicz; O Gawron; J C Sutherland
Related Documents :
9736156 - Analysis of tbpa and tbpb functionality in defective mutants of neisseria meningitidis.
1624426 - Effect of salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and p...
19778646 - Candidate verification of iron-regulated neisseria meningitidis proteins using isotopic...
11518716 - Three-dimensional model and characterization of the iron stress-induced cp43'-photosyst...
14592436 - A novel extracellular protein of streptomyces peucetius binds to daunorubicin but does ...
10524776 - The intermolecular disulfide bridge of human glial cell line-derived neurotrophic facto...
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    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aconitate Hydratase*
Animals
Circular Dichroism
Dithionite
Iron / analysis*
Iron-Sulfur Proteins*
Metalloproteins*
Myocardium / enzymology
Oxidation-Reduction
Protein Binding
Protein Conformation
Spectrophotometry
Sulfur / analysis*
Swine
Grant Support
ID/Acronym/Agency:
CA 00 465/CA/NCI NIH HHS; GM-26893/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Iron-Sulfur Proteins; 0/Metalloproteins; 14844-07-6/Dithionite; 7439-89-6/Iron; 7704-34-9/Sulfur; EC 4.2.1.3/Aconitate Hydratase

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


Previous Document:  On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transfo...
Next Document:  Lipids of synaptic vesicles: relevance to the mechanism of membrane fusion.