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Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purification, crystallization and preliminary X-ray analysis.
Coelho, Catarina; González, Pablo J; Trincão, José; Carvalho, Ana L; Najmudin, Shabir; Hettman, Thomas; Dieckman, Stephan; Moura, José J G; Moura, Isabel; Romão, Maria J.
Afiliación
  • Coelho C; REQUIMTE/CQFB, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal.
Article en En | MEDLINE | ID: mdl-17554176
ABSTRACT
The periplasmic nitrate reductase from Cupriavidus necator (also known as Ralstonia eutropha) is a heterodimer that is able to reduce nitrate to nitrite. It comprises a 91 kDa catalytic subunit (NapA) and a 17 kDa subunit (NapB) that is involved in electron transfer. The larger subunit contains a molybdenum active site with a bis-molybdopterin guanine dinucleotide cofactor as well as one [4Fe-4S] cluster, while the small subunit is a di-haem c-type cytochrome. Crystals of the oxidized form of this enzyme were obtained using polyethylene glycol 3350 as precipitant. A single crystal grown at the High Throughput Crystallization Laboratory of the EMBL in Grenoble diffracted to beyond 1.5 A at the ESRF (ID14-1), which is the highest resolution reported to date for a nitrate reductase. The unit-cell parameters are a = 142.2, b = 82.4, c = 96.8 A, beta = 100.7 degrees, space group C2, and one heterodimer is present per asymmetric unit.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Cupriavidus necator / Nitrato-Reductasa Idioma: En Revista: Acta Crystallogr Sect F Struct Biol Cryst Commun Año: 2007 Tipo del documento: Article País de afiliación: Portugal

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Cupriavidus necator / Nitrato-Reductasa Idioma: En Revista: Acta Crystallogr Sect F Struct Biol Cryst Commun Año: 2007 Tipo del documento: Article País de afiliación: Portugal