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Nitrate reductase (EC 1.7.1.1, EC 1.7.1.2, EC 1.7.1.3) catalyzes the NAD(P)H-dependent reduction of nitrate to nitrite. Eukaryotic assimilatory nitrate reductase catalyzes the following reaction:

NO₃- + NAD(P)H → NO₂- + NAD(P)⁺ + OH^-

Either NAD⁺ or NADP⁺ is the cofactor needed for nitrate reductase, and this enzyme can be further classified based on its cofactor preference: NADH-specific nitrate reductases (EC 1.7.7.1) exist in higher plants and algae; NADPH-specific nitrate reductases (EC 1.7.7.3) are found only in fungi; and NAD(P)H-bispecific nitrate reductases (EC 1.7.7.2) are found in higher plants, algae, and fungi. Nitrate reductase catalyzes the first step of nitrate assimilation in all these organisms, which is considered to be a rate-limiting process in acquisition of nitrogen in most cases. Each monomer of nitrate reductase consists of FAD, heme-iron, and molybdenum-molybdopterin (Mo-MPT). These components appear to act as the carriers in transferring electrons between the NAD(P)H oxidation site and the nitrate reduction site. Nitrate reductase is a multi-center redox protein that has three distinct domains: an N-terminal catalytic domain, which binds molybdopterin; a central domain, which is a cytochrome b557 sequence that binds haem; and a C-terminal domain, which is a cytochrome b reductase that binds FAD and a reduced pyridine nucleotide.

The physiological function of nitrate reductase is to catalyze pyridine nucleotide-dependent nitrate reduction as a component of the nitrogen-acquisition mechanism in higher plants, fungi, and algae. Nitrate reductase also plays a potential role in preserving and cleansing the environment by reducing excess nitrate and related nitrogen-containing nutrients in water sources. Despite its important functions, the activity assays of nitrate reductase using spectrophotometry have not been well established on an industrial scale, although activity measurement using other methods were reported before. Fortunately, supported by a professional team of extraordinary enzymologists, Creative Enzymes offers the most advanced spectrophotometric assay techniques to accurately measure the enzymatic activity of this enzyme. By constantly striving for products of utmost quality, Creative Enzymes has emerged as a worldwide leader in providing services for enzymatic activity quantification. Overall, Creative Enzymes will always support your aim at notable achievements with our specialized services.

Figure: The crystal structure of nitrate reductase (NADPH) from Ogataea angusta.
PDB: 2BIH