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Literature summary for 1.9.6.1 extracted from

  • Jepson, B.J.; Mohan, S.; Clarke, T.A.; Gates, A.J.; Cole, J.A.; Butler, C.S.; Butt, J.N.; Hemmings, A.M.; Richardson, D.J.
    Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli (2006), J. Biol. Chem., 282, 6425-6437.
    View publication on PubMed
Search for more literature for 1.9.6.1

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion method Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe NapA contains a [4Fe-4S] cluster Escherichia coli
Mo5+ NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor. The molybdenum ion coordination sphere of NapA includes two molybdopterin guanine dinucleotide dithiolenes, a protein-derived cysteinyl ligand and an oxygen atom. The Mo-O bond length is 2.6 A, which is indicative of a water ligand. In NapA or NapAB, the Mo5+ state can not be further reduced to Mo4+. A catalytic cycle for NapA is proposed in which nitrate binds to the Mo5+ ion and where a stable des-oxo Mo6+ species may participate Escherichia coli
Mo6+ NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor. The molybdenum ion coordination sphere of NapA includes two molybdopterin guanine dinucleotide dithiolenes, a protein-derived cysteinyl ligand and an oxygen atom. The Mo-O bond length is 2.6 A, which is indicative of a water ligand. In NapA or NapAB, the Mo5+ state can not be further reduced to Mo4+. A catalytic cycle for NapA is proposed in which nitrate binds to the Mo5+ ion and where a stable des-oxo Mo6+ species may participate Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
 1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively Escherichia coli
90000
-
 1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
of NapA and NapB Escherichia coli

Subunits

Subunits Comment Organism
? 1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively Escherichia coli

Synonyms

Synonyms Comment Organism
NapA
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
bis(molybdopterin guanine dinucleotide)molybdenum cofactor NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor Escherichia coli
heme the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB) Escherichia coli