Literature summary for 1.7.2.1 extracted from

Sato, K.; Firbank, S.J.; Li, C.; Banfield, M.J.; Dennison, C.
The importance of the long type 1 copper-binding loop of nitrite reductase for structure and function (2008), Chemistry, 14, 5820-5828.

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Protein Variants

Protein Variants	Comment	Organism
additional information	replacement of the long 15-residue type 1 copper-binding loop of nitrite reductase with that from Paracoccus versutus cupredoxin amicyanin. The sizable loop contraction does not have a significant effect on the structures of both the type 1 and type 2 CuII sites. The crystal structure of the variant with ZnII at both the type 1 and type 2 sites shows a coordination geometry of the type 2 site that is almost identical to that found in the wild-type protein. In the type 1 centre, the positions of most of the coordinating residues are altered with the largest difference observed for the coordinating His residue in the centre of the mutated loop. This ligand moves away from the active site, which results in a more open metal centre with a coordinating water molecule. The reduction potential of the type i centre is reduced by 200 mV. The resulting unfavourable driving force for electron transfer between the two copper sites, and an increased reorganisation energy for the type 1 centre, contribute to the loop variant having very little nitrite reductase activity	Achromobacter xylosoxidans

Organism

Organism	UniProt	Comment	Textmining
Achromobacter xylosoxidans	O68601	-	-

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Release 2023.1 (January 2023)