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Literature summary for 1.7.2.1 extracted from

  • Radoul, M.; Centola, F.; Rinaldo, S.; Cutruzzola, F.; Pecht, I.; Goldfarb, D.
    Heme d1 nitrosyl complex of cd1 nitrite reductase studied by high-field-pulse electron paramagnetic resonance spectroscopy (2009), Inorg. Chem., 48, 3913-3915.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y10F high-field-pulse electron papramagnetic spectroscopy spectra and the derived 14N hyperfine and quadrupole interactions are the same for wild-type and mutant. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Synonyms

Synonyms Comment Organism
cd1 nitrite reductase
-
Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
heme characterization of the nitrosyl d1 heme complex by high-field-pulse electron papramagnetic spectroscopy spectra and derived 14N hyperfine and quadrupole interactions. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution Pseudomonas aeruginosa