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The interaction of ferredoxin‐linked sulfite reductase with ferredoxin
Author(s) -
Hirasawa Masakazu,
Boyer J.Milton,
Gray Kevin A.,
Davis Danny J.,
Knaff David B.
Publication year - 1987
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(87)80953-5
Subject(s) - ferredoxin , sulfite reductase , spinach , reductase , sulfite , ferredoxin—nadp(+) reductase , chemistry , ionic strength , ferredoxin thioredoxin reductase , enzyme , biochemistry , size exclusion chromatography , organic chemistry , thioredoxin reductase , aqueous solution , glutathione
Spinach sulfite reductase has been shown to co‐migrate during gel filtration chromatography at low ionic strength with spinach ferredoxin. No co‐migration was observed at high ionic strength. These results indicate that the two proteins form a high‐affinity, electrostatically stabilized complex, as had previously been demonstrated for three other ferredoxin‐dependent, plant enzymes. Modification of 3–4 ferredoxin carboxyl groups had little detectable effect on the ferredoxin‐sulfite reductase interaction.