Abstract
When extracts of Anabaena cylindrica are prepared in the absence of dithionite, they catalyze pyruvate-dependent acetylene reduction, a reaction not observable in assays containing dithionite. Ferredoxin and coenzyme-A, but not NADP and ferredoxin-NADP reductase, are required for maximal pyruvate-dependent activity. These acetylene-reducing extracts do not exhibit NADP-pyruvate dehydrogenase activity. However, pyruvate:ferredoxin oxidoreductase is present at levels of activity sufficient to support the in vitro rate of pyruvate-supported acetylene reduction. These in vitro data support earlier in vivo evidence that pyruvate:ferredoxin oxidoreductase transfers electrons from pyruvate to nitrogenase in A. cylindrica .
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More From: Biochemical and Biophysical Research Communications
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