Abstract
NADH-nitrate reductase (NR) from barley ( Hordeum vulgare L. cv. Steptoe) leaves was purified to specific activity of 19 μmol NO 2 − produced per min per mg protein with 27% yield by blue A sepharose affinity chromatography. Reduction of NR by NADH resulted in spectral absorption maxima at 422 (γ), 528 (β) and 556 (α) nm while oxidation by nitrate caused disappearance of α and β peaks and a shift of the γ peak to 413 nm. These results demonstrate the presence of a functional cytochrome b 557 in barley nitrate reductase.
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