The PSI-E subunit of photosystem I binds ferredoxin:NADP + oxidoreductase

A photosystem I complex containing the polypeptides PSI-A to PSI-L, light-harvesting complex I and ferredoxin:NADP + oxidoreductase has been isolated from barley using the non-ionic detergent n-decyl-β- d-maltopyranoside. The ratio between bound forredoxin:NADP + oxidoreductase and P700 is 0.4 ± 0.2...

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Bibliographic Details
Published inFEBS letters Vol. 311; no. 2; pp. 169 - 173
Main Authors Andersen, Birgitte, Scheller, Henrik Vibe, Møller, Birger Lindberg
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 19.10.1992
Elsevier
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Summary:A photosystem I complex containing the polypeptides PSI-A to PSI-L, light-harvesting complex I and ferredoxin:NADP + oxidoreductase has been isolated from barley using the non-ionic detergent n-decyl-β- d-maltopyranoside. The ratio between bound forredoxin:NADP + oxidoreductase and P700 is 0.4 ± 0.2. The complex is highly active in catalyzing light-induced transfer of electrons from plastocyanin to NADP + at rates of 280±150 and 1800 ± 800, μmol NADPH/(mg chl h), without and in the presence of saturating amounts of exogenously added ferredoxin:NADP + oxidoreductase, respectively. Endogenously bound ferredoxin:NADP + oxidoreductase interacts with the PSI-E subunit as demonstrated by cross-linking experiments using two different types of cross-linkers and identification of the products by Western blotting and the use of monospecific antibodies.
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content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81391-X