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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Published in | FEBS letters Vol. 311; no. 2; pp. 169 - 173 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
19.10.1992
Elsevier |
Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(92)81391-X |