X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus

Journal of Biological Chemistry

Volumn 275, Issue 33, 2000, Pages 25089-25094

  Jafferji, A ^a   Allen, J W A ^a   Ferguson, S J ^a   Fulop, V ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYANIDE; CYTOCHROME; FERROUS ION; HEME; NITRITE REDUCTASE;

ARTICLE; CHEMICAL BINDING; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; OXIDATION; PARACOCCUS; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

ANIONS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYANIDES; CYTOCHROMES; ELECTRON TRANSPORT COMPLEX IV; HEME; HYDROGEN BONDING; KINETICS; LIGANDS; MODELS, MOLECULAR; NITRITE REDUCTASES; OXIDATION-REDUCTION; PARACOCCUS; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; PARACOCCUS PANTOTROPHUS;

EID: 0034682829     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M001377200     Document Type: Article

References (43)

1. Collaborative Computational Project, No 4