1ZV2

Cu-containing nitrite reductase

Summary for 1ZV2

• Entry DOI: 10.2210/pdb1zv2/pdb
• Descriptor: Copper-containing nitrite reductase, COPPER (II) ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: copper protein, nitrite reduction, denitrification, oxidoreductase
• Biological source: Rhodobacter sphaeroides
• Cellular location: Periplasm : Q53239
• Total number of polymer chains: 1
• Total formula weight: 35998.49

Authors

Jacobson, F.,Guo, H.,Olesen, K.,Okvist, M.,Neutze, R.,Sjolin, L. (deposition date: 2005-06-01, release date: 2005-06-21, Last modification date: 2023-08-23)

Primary citation

Jacobson, F.,Guo, H.,Olesen, K.,Okvist, M.,Neutze, R.,Sjolin, L.
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.
Acta Crystallogr.,Sect.D, 61:1190-1198, 2005

PubMed 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.

PubMed: 16131751
DOI: 10.1107/S0907444905017488

Experimental method

X-RAY DIFFRACTION (1.74 Å)