Document Detail

Studies of the ferredoxin from Thermus thermophilus.
MedLine Citation:
PMID:  6313685     Owner:  NLM     Status:  MEDLINE    
The soluble ferredoxin from Thermus thermophilus was examined by Mössbauer and EPR spectroscopies and by reductive titrations. These studies demonstrate the presence of one 3Fe center, responsible for the characteristic g = 2.02 EPR signal in the oxidized protein, and one [4Fe-4S] center which is responsible for the rhombic EPR spectrum of the fully reduced protein. These assignments should replace those made by Ohnishi et al. (Ohnishi, T., Blum, H., Sato, S., Nakazawa, K., Hon-nami, K., and Oshima, T. (1980) J. Biol. Chem. 255, 345-348) prior to the discovery of the 3Fe clusters. The amino acid composition was determined and is discussed with reference to recent structural studies of 7Fe ferredoxins.
R Hille; T Yoshida; G E Tarr; C H Williams; M L Ludwig; J A Fee; T A Kent; B H Huynh; E Münck
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  258     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1983 Nov 
Date Detail:
Created Date:  1983-12-17     Completed Date:  1983-12-17     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  13008-13     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
Electron Spin Resonance Spectroscopy
Ferredoxin-NADP Reductase / metabolism
Ferredoxins / isolation & purification*,  metabolism
Iron / analysis
Plants / enzymology
Spectrum Analysis
Thermus / metabolism*
Grant Support
Reg. No./Substance:
0/Amino Acids; 0/Ferredoxins; 7439-89-6/Iron; EC Reductase

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

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