Abstract
Summary An iron-sulfur protein containing eight iron atoms and eight acid-labile sulfur atoms per one molecule of 19,000 daltons was found in Pseudomonas ovalis which had been grown on medium supplemented with glucose and ammonium sulfate. This protein molecule was composed of two subunits of identical size. The absorption spectrum exhibited a peak at 283 nm with shoulders at 320 nm and 400 nm. The purified iron-sulfur protein catalyzed the photorenduction of NAFP by spinach chloroplast.
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More From: Biochemical and Biophysical Research Communications
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