The Covalent Structure of the Blue Copper-Containing Nitrite Reductase fromAchromobacter xylosoxidans

1998 ◽  
Vol 247 (3) ◽  
pp. 734-740 ◽  
Author(s):  
Isabel H.M. Vandenberghe ◽  
Terrance E. Meyer ◽  
Michael A. Cusanovich ◽  
Jozef J. Van Beeumen
Keyword(s):  
Nitrite Reductase ◽  
Blue Copper ◽  
Covalent Structure

X-ray structure of a blue copper nitrite reductase at high pH and in copper-free form at 1.9 Å resolution

2001 ◽  
Vol 57 (8) ◽  
pp. 1110-1118 ◽  
Author(s):  
Mark J. Ellis ◽  
Fraser E. Dodd ◽  
Richard W. Strange ◽  
Miguel Prudêncio ◽  
Gary Sawers ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Free Form ◽  
Blue Copper ◽  
X Ray ◽  
High Ph

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.

Spectroscopic evidence for a copper-nitrosyl intermediate in nitrite reduction by blue copper-containing nitrite reductase

1989 ◽  
Vol 164 (3) ◽  
pp. 1366-1372 ◽  
Author(s):  
Shinnichiro Suzuki ◽  
Tetsuhiko Yoshimura ◽  
Takamitsu Kohzuma ◽  
Sohsuke Shidara ◽  
Masayuki Masuko ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Nitrite Reduction ◽  
Blue Copper ◽  
Spectroscopic Evidence

scholarly journals XAFS and crystallographic studies of an azurin and a blue copper nitrite reductase from a denitrifying bacterium

1996 ◽  
Vol 52 (a1) ◽  
pp. C70-C70
Author(s):  
S. S. Hasnain ◽  
F. Dodd ◽  
R. Strange ◽  
G. Grossmann ◽  
L. Murphy ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Blue Copper ◽  
Denitrifying Bacterium

scholarly journals Electronic Structure of the Perturbed Blue Copper Site in Nitrite Reductase:  Spectroscopic Properties, Bonding, and Implications for the Entatic/Rack State

1996 ◽  
Vol 118 (33) ◽  
pp. 7755-7768 ◽  
Author(s):  
Louis B. LaCroix ◽  
Susan E. Shadle ◽  
Yaning Wang ◽  
Bruce A. Averill ◽  
Britt Hedman ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Nitrite Reductase ◽  
Spectroscopic Properties ◽  
Blue Copper ◽  
Copper Site
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