Abstract
— Nitrate reductases (NR) from NR-normal Neurospora crassa mutant albino band and from NR-defective mutantsnit–1 andnit–3 were isolated and partially purified in order to test the photo-reducibility of their cytochrome b557 via the NR-internal FAD. Photoreducibility with blue light of the isolated enzyme was observed as absorbance increase at 423, 524 and553–557 nm. It was independent of NADPH-nitrate reductase activity and could be induced if the dissociable FAD was not lost in the isolation procedure. The photoreduction of cytochrome b557 was readily reversible due the high autoxi-dation rate of this cytochrome. Therefore, anaerobic conditions are required for photoreduction with low light intensities. If aerobic conditions are applied, high intensities become necessary to overcome the simultaneous cytochrome h557 oxidation.
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