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Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: changes in the interactions of the type 2 copper.

Jacobson F, Guo H, Olesen K, Okvist M, Neutze R, Sjölin L
Acta Crystallogr D Biol Crystallogr 61 1190-8 (2005)
Cited: 16 times
EuropePMC logo PMID: 16131751

Abstract

Nitrite reductase is an enzyme operating in the denitrification pathway which catalyses the conversion of nitrite (NO2(-)) to gaseous nitric oxide (NO). Here, crystal structures of the oxidized and reduced forms of the copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3 are presented at 1.74 and 1.85 A resolution, respectively. Whereas the structure of the enzyme is very similar to those of other copper-containing nitrite reductases, folding as a trimer and containing two copper sites per monomer, the structures reported here enable conformational differences between the oxidized and reduced forms of the enzyme to be identified. In the type 1 copper site, a rotational perturbation of the side chain of the copper ligand Met182 occurs upon reduction. At the type 2 copper site, a dual conformation of the catalytic residue His287 is observed in the oxidized structure but is lacking in the reduced structure, such that the interactions of the oxidized type 2 copper ion can be regarded as adopting octahedral geometry. These findings shed light on the structural mechanism of the reduction of a copper-bound nitrite to nitric oxide and water.

Articles - 1zv2 mentioned but not cited (5)

  1. Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins. Lawton TJ, Sayavedra-Soto LA, Arp DJ, Rosenzweig AC. J Biol Chem 284 10174-10180 (2009)
  2. Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function. Ghosh S, Xie X, Dey A, Sun Y, Scholes CP, Solomon EI. Proc Natl Acad Sci U S A 106 4969-4974 (2009)
  3. Highly diverse nirK genes comprise two major clades that harbour ammonium-producing denitrifiers. Helen D, Kim H, Tytgat B, Anne W. BMC Genomics 17 155 (2016)
  4. Characterization of a nitrite reductase involved in nitrifier denitrification. Lawton TJ, Bowen KE, Sayavedra-Soto LA, Arp DJ, Rosenzweig AC. J Biol Chem 288 25575-25583 (2013)
  5. The Rise of Radicals in Bioinorganic Chemistry. Gray HB, Winkler JR. Isr J Chem 56 640-648 (2016)


Reviews citing this publication (1)

  1. Recent structural insights into the function of copper nitrite reductases. Horrell S, Kekilli D, Strange RW, Hough MA. Metallomics 9 1470-1482 (2017)

Articles citing this publication (10)



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