Structure and function of eukaryotic NAD(P)H:nitrate reductase

Pyridine nucleotide-dependent nitrate reductases (NRs; EC 1.6.6.1-3) are molybdenum-containing enzymes found in eukaryotic organisms which assimilate nitrate. NR is a homodimer with an approximately 100 kDa polypeptide which folds into stable domains housing each of the enzyme's redox cofactors...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2001-02, Vol.58 (2), p.194-204
Main Author: Campbell, W H
Format: Article
Language:English
Subjects:
Catalysis
Catalytic Domain
Enzymes
Eukaryotes
Eukaryotic Cells - enzymology
Holoenzymes - chemistry
Holoenzymes - genetics
Holoenzymes - metabolism
Molecular biology
Molybdenum
Mutagenesis
Nitrate Reductase (NAD(P)H)
Nitrate Reductases - chemistry
Nitrate Reductases - genetics
Nitrate Reductases - metabolism
Nitrates
Oxidation-Reduction
Pichia pastoris
Plant biology
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
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Summary:Pyridine nucleotide-dependent nitrate reductases (NRs; EC 1.6.6.1-3) are molybdenum-containing enzymes found in eukaryotic organisms which assimilate nitrate. NR is a homodimer with an approximately 100 kDa polypeptide which folds into stable domains housing each of the enzyme's redox cofactors--FAD, heme-Fe molybdopterin (Mo-MPT) and the electron donor NAD(P)H--and there is also a domain for the dimer interface. NR has two active sites: the nitrate-reducing Mo-containing active site and the pyridine nucleotide active site formed between the FAD and NAD(P)H domains. The major barriers to defining the mechanism of catalysis for NR are obtaining the detailed three-dimensional structures for oxidized and reduced enzyme and more in-depth analysis of electron transfer rates in holo-NR. Recombinant expression of holo-NR and its fragments, including site-directed mutagenesis of key acative site and domain interface residues, are expected to make large contributions to this effort to understand the catalytic mechanism of NR.
ISSN:1420-682X
1420-9071
DOI:10.1007/PL00000847