rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
2003-6-30
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pubmed:abstractText |
In order to elucidate the importance of a ferredoxin (Fd) Arg-Glu pair involved in dynamic exchange from intra- to intermolecular salt bridges upon complex formation with ferredoxin-NADP(+) oxidoreductase (FNR), Equisetum arvense FdI and FdII were investigated as normal and the pair-lacking Fd, respectively. The FdI mutant lacking this pair was unstable and rapidly lost the [2Fe-2S] cluster. The catalytic constant (k(cat)) of the electron transfer for FdI is 5.5 times that for FdII and the introduction of this pair into FdII resulted in the increase of k(cat) to a level comparable to that for FdI, demonstrating directly that the Arg-Glu pair is important for efficient electron transfer between Fd and FNR.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
546
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
189-94
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pubmed:meshHeading |
pubmed-meshheading:12832038-Amino Acid Sequence,
pubmed-meshheading:12832038-Arginine,
pubmed-meshheading:12832038-Base Sequence,
pubmed-meshheading:12832038-DNA Primers,
pubmed-meshheading:12832038-Electron Transport,
pubmed-meshheading:12832038-Ferredoxin-NADP Reductase,
pubmed-meshheading:12832038-Ferredoxins,
pubmed-meshheading:12832038-Glutamic Acid,
pubmed-meshheading:12832038-Molecular Sequence Data,
pubmed-meshheading:12832038-Recombinant Proteins,
pubmed-meshheading:12832038-Sequence Homology, Amino Acid
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pubmed:year |
2003
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pubmed:articleTitle |
A ferredoxin Arg-Glu pair important for efficient electron transfer between ferredoxin and ferredoxin-NADP(+) reductase.
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pubmed:affiliation |
Faculty of Integrated Arts and Sciences, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima 739-8521, Japan. teshi@hiroshima-u.ac.jp
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pubmed:publicationType |
Journal Article
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