PMID: 1637357Jul 15, 1992Paper

Expression of Pseudomonas aeruginosa nitrite reductase in Pseudomonas putida and characterization of the recombinant protein

The Biochemical Journal
M C SilvestriniE Zennaro

Abstract

Nitrite reductase from Pseudomonas aeruginosa has been successfully expressed in Pseudomonas putida. The purified recombinant enzyme contains haem c but no haem d1. Nonetheless, like the holoenzyme from Ps. aeruginosa, it is a stable dimer (molecular mass 120 kDa), and electron transfer to oxidized azurin is biphasic and follows bimolecular kinetics (k1 = 1.5 x 10(5) and k2 = 2.2 x 10(4) M-1.s-1). Unlike the chemically produced apoenzyme, recombinant nitrite reductase containing only haem c is water-soluble, stable at neutral pH and can be quantitatively reconstituted with haem d1, yielding a holoenzyme with the same properties as that expressed by Ps. aeruginosa (namely optical and c.d. spectra, molecular mass, cytochrome c551 oxidase activity and CO-binding kinetics).

Citations

Aug 15, 2014·Biochemical and Biophysical Research Communications·Serena RinaldoFrancesca Cutruzzolà
May 13, 1999·Biochimica Et Biophysica Acta·F Cutruzzolà
Apr 4, 2014·Chemical Reviews·Luisa B Maia, José J G Moura
Feb 28, 2001·Proceedings of the National Academy of Sciences of the United States of America·F CutruzzolaM Brunori
Sep 21, 2001·Journal of Molecular Biology·K BrownM Tegoni
Jun 1, 2001·Methods : a Companion to Methods in Enzymology·A BellelliM T Wilson
Feb 7, 2002·Biochemical and Biophysical Research Communications·Wenliang SunFrancesca Cutruzzolà
May 28, 2003·Protein Expression and Purification·Gregory T MillerRussell Timkovich
Dec 31, 1997·Microbiology and Molecular Biology Reviews : MMBR·W G Zumft
Feb 12, 2011·Journal of the American Chemical Society·Marina RadoulDaniella Goldfarb

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