| Human ferredoxin-2 displays a unique conformational change. | |
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MedLine Citation:
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PMID: 23208207 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Wenbin Qi; Jingwei Li; J A Cowan |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-12-3 |
Journal Detail:
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Title: Dalton transactions (Cambridge, England : 2003) Volume: - ISSN: 1477-9234 ISO Abbreviation: Dalton Trans Publication Date: 2012 Dec |
Date Detail:
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Created Date: 2012-12-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101176026 Medline TA: Dalton Trans Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. cowan@chemistry.ohio-state.edu. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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