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Literature summary for 1.7.2.1 extracted from

  • Hough, M.A.; Ellis, M.J.; Antonyuk, S.; Strange, R.W.; Sawers, G.; Eady, R.R.; Samar Hasnain, S.
    High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase (2005), J. Mol. Biol., 350, 300-309.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapour diffusion method. Crystal structures of M144L and M144Q at 1.9 A, crystal structure of native enzyme at 1.04 A, structure of mutant enzyme C130A at 1.35 A Achromobacter xylosoxidans

Protein Variants

Protein Variants Comment Organism
C130A inactive mutant enzyme, the loss of activity in this mutant is due to the absence of T1Cu and loss of the Cu–Cys130Sg bond rather than any change to the protein structure in this region Achromobacter xylosoxidans
M144L change in activity in the mutant is related to the perturbation of the finely poised redox potentials of the T1Cu sites of azurin and AxNiR Achromobacter xylosoxidans
M144Q change in activity in the mutant is related to the perturbation of the finely poised redox potentials of the T1Cu sites of azurin and AxNiR Achromobacter xylosoxidans

Organism

Organism UniProt Comment Textmining
Achromobacter xylosoxidans
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Synonyms

Synonyms Comment Organism
AxNiR
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 Achromobacter xylosoxidans