Abstract
Here we investigate the structure of the two types of copper site in nitrite reductase from Alcaligenes xylosoxidans, the molecular organisation of the enzyme when the type-2 copper is absent, and its mode of substrate binding. X-ray absorption studies provide evidence for a fourth ligand at the type-2 Cu, that substrate binds to this site and indicates that this binding does not change the type-1 Cu centre. The substrate replaces a putative water ligand and is accommodated by a lengthening of the Cu–histidine bond by approximately 0.08 Å. Modelling suggests a similarity between this unusual type-2 Cu site and the Zn site in carbonic anhydrase and that nitrite is anchored by hydrogen bonds to an unligated histidine present in the type-2 Cu cavity.
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Strange, R., Dodd, F., Abraham, Z. et al. The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase. Nat Struct Mol Biol 2, 287–292 (1995). https://doi.org/10.1038/nsb0495-287
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DOI: https://doi.org/10.1038/nsb0495-287
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