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Association of ferredoxin‐NADP + oxidoreductase with the chloroplast cytochrome b‐f complex
Author(s) -
Clark R.D.,
Hawkesford M.J.,
Coughlan S.J.,
Bennett J.,
Hind G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81092-3
Subject(s) - ferredoxin , oxidoreductase , thylakoid , ferredoxin—nadp(+) reductase , cytochrome , cytochrome b6f complex , chloroplast , cyanogen bromide , chemistry , biochemistry , cytochrome c , reductase , stereochemistry , enzyme , peptide sequence , mitochondrion , gene
The 37‐kDa non‐heme component in spinach cytochrome b‐f complex prepared from EDTA‐washed thylakoids [(1983) J. Biol. Chem. 258, 10348‐10354] is shown to be ferredoxin‐NADP + oxidoreductase (EC 1.18.1.2) on the basis of immunoreactivity, amino acid analysis, and pattern of cleavage by cyanogen bromide. Strong binding of the reductase to the isolated cytochrome complex suggests this is an important site for its attachment to the thylakoid membrane in vivo.