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1987•FEBS LettersRequires access

The interaction of ferredoxin‐linked sulfite reductase with ferredoxin

Masakazu Hirasawa, J.Milton Boyer, Kevin A. Gray, Danny J. Davis, David B. Knaff

Open publisher page 13 citations

Abstract

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.

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What this paper is about

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.

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Available abstract

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.

Key concepts: Ferredoxin, Sulfite reductase, Spinach, Reductase, Sulfite, Ferredoxin—NADP(+) reductase, Chemistry, Ionic strength

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