Document Detail


Human ferredoxin-2 displays a unique conformational change.
MedLine Citation:
PMID:  23208207     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human ferredoxin-1 (hFd1) and human ferredoxin-2 (hFd2) share high sequence similarity but serve on distinct cellular pathways. A unique conformational change is observed when holo hFd2 is warmed to physiological temperatures, or higher. Enzymatic studies show that this conformational change causes the increase of affinity between hFd2 and adrenodoxin reductase. No such change was observed for hFd1, which may contribute to the distinct cellular functions of hFd1 and hFd2 under physiological conditions.
Authors:
Wenbin Qi; Jingwei Li; J A Cowan
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-12-03
Journal Detail:
Title:  Dalton transactions (Cambridge, England : 2003)     Volume:  42     ISSN:  1477-9234     ISO Abbreviation:  Dalton Trans     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-02-06     Completed Date:  2013-07-29     Revised Date:  2014-03-09    
Medline Journal Info:
Nlm Unique ID:  101176026     Medline TA:  Dalton Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  3088-91     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Ferredoxins / chemistry*,  metabolism*
Humans
Protein Conformation
Temperature
Grant Support
ID/Acronym/Agency:
AI072443/AI/NIAID NIH HHS; R21 AI072443/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Ferredoxins
Comments/Corrections

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


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