Literature summary 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.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.7.2.1	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

EC Number	Organism	UniProt	Comment	Textmining
1.7.2.1	Pseudomonas aeruginosa	-	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.7.2.1	cd1 nitrite reductase	-	Pseudomonas aeruginosa

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.7.2.1	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

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Release 2023.1 (January 2023)