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• W1968076970 abstract "Nitrite reductase is an enzyme operating in the denitrification pathway which catalyses the conversion of nitrite (NO_{2}^{-}) 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 Å 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." @default.
• W1968076970 created "2016-06-24" @default.
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• W1968076970 date "2005-08-16" @default.
• W1968076970 modified "2023-10-12" @default.
• W1968076970 title "Structures of the oxidized and reduced forms of nitrite reductase from<i>Rhodobacter sphaeroides</i>2.4.3 at high pH: changes in the interactions of the type 2 copper" @default.
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• W1968076970 doi "https://doi.org/10.1107/s0907444905017488" @default.
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