The reductive reaction mechanism of tobacco nitrite reductase derived from a combination of crystal structures and ultraviolet-visible microspectroscopy

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 8, 2012, Pages 2035-2045

  Nakano, Shogo ^a   Takahashi, Misa ^a   Sakamoto, Atsushi ^a   Morikawa, Hiromichi ^a   Katayanagi, Katsuo ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Assimilatory nitrite reductase; N O bond cleavage; Nii3; Radiation induced reaction; Reaction mechanism; UV Vis microspectroscopy; X ray crystallography

Indexed keywords

ARGININE; ASSIMILATORY NITRITE REDUCTASE; LYSINE; NITRITE; NITRITE REDUCTASE; NITROGEN; NITROGEN DIOXIDE; OXYGEN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL BOND; CHEMICAL INTERACTION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; GEOMETRY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RADIATION EXPOSURE; REDUCTION; TOBACCO; ULTRAVIOLET SPECTROSCOPY; ULTRAVIOLET VISIBLE MICROSPECTROSCOPY; X IRRADIATION;

AMINO ACIDS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HEME; LIGANDS; NITRIC OXIDE; NITRITE REDUCTASES; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ULTRAVIOLET; TOBACCO;

NICOTIANA TABACUM;

EID: 84863779142     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24094     Document Type: Article

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