CuI and CuII Complexes Containing Nitrite and Tridentate Aromatic Amine Ligand as Models for the Substrate-Binding Type-2 Cu Site of Nitrite Reductase

2005 ◽  
Vol 2005 (8) ◽  
pp. 1435-1441 ◽  
Author(s):  
Hiroshi Yokoyama ◽  
Kazuya Yamaguchi ◽  
Manabu Sugimoto ◽  
Shinnichiro Suzuki
Keyword(s):  
Aromatic Amine ◽  
Nitrite Reductase ◽  
Substrate Binding ◽  
Binding Type ◽  
Amine Ligand

Characterization of Azide-Binding Type 2 Cu(II) Site of Nitrite Reductase

2001 ◽  
Vol 74 (1) ◽  
pp. 183-184
Author(s):  
Kunishige Kataoka ◽  
Shinnichiro Suzuki
Keyword(s):  
Nitrite Reductase ◽  
Azide Binding ◽  
Binding Type

scholarly journals A Highly Efficient Aromatic Amine Ligand/Copper(I) Chloride Catalyst System for the Synthesis of Poly(2,6-dimethyl-1,4-phenylene ether)

Polymers ◽  
2018 ◽  
Vol 10 (4) ◽  
pp. 350 ◽  
Author(s):  
Kisoo Kim ◽  
Min Shin ◽  
Yong Kim ◽  
Joong-In Kim ◽  
Young Kim
Keyword(s):  
Aromatic Amine ◽  
Catalyst System ◽  
Highly Efficient ◽  
Chloride Catalyst ◽  
Amine Ligand

scholarly journals The Blue Copper-Containing Nitrite Reductase fromAlcaligenes xylosoxidans: Cloning of the nirAGene and Characterization of the Recombinant Enzyme

1999 ◽  
Vol 181 (8) ◽  
pp. 2323-2329 ◽  
Author(s):  
Miguel Prudêncio ◽  
Robert R. Eady ◽  
Gary Sawers
Keyword(s):  
Amino Acid ◽  
Nitrite Reductase ◽  
Recombinant Enzyme ◽  
Leader Peptide ◽  
Resonance Spectroscopy ◽  
Gene Encoding ◽  
Blue Copper

ABSTRACT The nirA gene encoding the blue dissimilatory nitrite reductase from Alcaligenes xylosoxidans has been cloned and sequenced. To our knowledge, this is the first report of the characterization of a gene encoding a blue copper-containing nitrite reductase. The deduced amino acid sequence exhibits a high degree of similarity to other copper-containing nitrite reductases from various bacterial sources. The full-length protein included a 24-amino-acid leader peptide. The nirA gene was overexpressed inEscherichia coli and was shown to be exported to the periplasm. Purification was achieved in a single step, and analysis of the recombinant Nir enzyme revealed that cleavage of the signal peptide occurred at a position identical to that for the native enzyme isolated from A. xylosoxidans. The recombinant Nir isolated directly was blue and trimeric and, on the basis of electron paramagnetic resonance spectroscopy and metal analysis, possessed only type 1 copper centers. This type 2-depleted enzyme preparation also had a low nitrite reductase enzyme activity. Incubation of the periplasmic fraction with copper sulfate prior to purification resulted in the isolation of an enzyme with a full complement of type 1 and type 2 copper centers and a high specific activity. The kinetic properties of the recombinant enzyme were indistinguishable from those of the native nitrite reductase isolated from A. xylosoxidans. This rapid isolation procedure will greatly facilitate genetic and biochemical characterization of both wild-type and mutant derivatives of this protein.

Effect of Arginine at Type 2 Cu Site on Spectroscopic Features and Enzymatic Activity of Copper-containing Nitrite Reductase

2007 ◽  
Vol 36 (1) ◽  
pp. 140-141
Author(s):  
Kazuya Yamaguchi ◽  
Aiko Tsuda ◽  
Masaki Nojiri ◽  
Shinnichiro Suzuki
Keyword(s):  
Enzymatic Activity ◽  
Nitrite Reductase

The nature of the substrate binding site in copper nitrite reductase from Achromobacter xylosoxidans (AxNiR)

1995 ◽  
Vol 59 (2-3) ◽  
pp. 711
Author(s):  
R.W. Strange ◽  
J.G. Grossmann ◽  
F.E. Dodd ◽  
S.S. Hasnain ◽  
Z.H.L. Abraham ◽  
...  
Keyword(s):  
Binding Site ◽  
Nitrite Reductase ◽  
Substrate Binding ◽  
Achromobacter Xylosoxidans ◽  
Substrate Binding Site

Substrate Binding to a Nitrite Reductase Induces a Spin Transition

2010 ◽  
Vol 114 (16) ◽  
pp. 5563-5566 ◽  
Author(s):  
Gabriel Martins ◽  
Luisa Rodrigues ◽  
Filipa M. Cunha ◽  
Daniela Matos ◽  
Peter Hildebrandt ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Substrate Binding ◽  
Spin Transition
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