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Literature summary for 1.7.2.1 extracted from

  • Wijma, H.J.; MacPherson, I.; Farver, O.; Tocheva, E.I.; Pecht, I.; Verbeet, M.P.; Murphy, M.E.; Canters, G.W.
    Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase (2007), J. Am. Chem. Soc., 129, 519-525.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
M150G crystals are grown at room temperature by hanging drop vapor diffusion method Alcaligenes faecalis

Protein Variants

Protein Variants Comment Organism
M150G mutation increases the reorganization energy by 0.3 eV (30 kJ/mol), binding of the nearby Met62 to the type-1 Cu site lowers the reorganization energy back to approximately the wild-type value Alcaligenes faecalis
M150T mutation increases the reorganization energy by 0.3 eV (30 kJ/mol) Alcaligenes faecalis

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis
-
S-6
-
Alcaligenes faecalis S-6
-
S-6
-