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Crystal structures of ferredoxin variants exhibiting large changes in [Fe-S] reduction potential.

Abstract:

Elucidating how proteins control the reduction potentials (E0') of [Fe--S] clusters is a longstanding fundamental problem in bioinorganic chemistry. Two site-directed variants of Azotobacter vinelandii ferredoxin I (FdI) that show large shifts in [Fe--S] cluster E0' (100--200 mV versus standard hydrogen electrode (SHE)) have been characterized. High resolution X-ray structures of F2H and F25H variants in their oxidized forms, and circular dichroism (CD) and electron paramagnetic resonance (EP...

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Publication status:
Published

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Publisher copy:
10.1038/nsb751

Authors


Bonagura, CA More by this author
Tilley, GJ More by this author
McEvoy, JP More by this author
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Journal:
Nature structural biology
Volume:
9
Issue:
3
Pages:
188-192
Publication date:
2002-03-05
DOI:
ISSN:
1072-8368
URN:
uuid:a5b845e1-4d97-4c2b-9cba-4a91dc464202
Source identifiers:
38193
Local pid:
pubs:38193

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