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|Título: ||Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purification, crystallization and preliminary X-ray analysis|
|Autor: ||Coelho, Catarina|
J. Gonzaléz, Pablo
Carvalho, Ana L.
Moura, José J. G.
Romão, Maria J.
|Issue Date: ||2007|
|Editora: ||International Union of Crystallography|
|Resumo: ||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 ° , ß = 100.7°, space group C2, and one heterodimer is present per asymmetric unit.|
|Descrição: ||Acta Cryst. (2007). F63, 516–519|
|Appears in Collections:||FCT: DQ - Artigos em revista internacional com arbitragem científica|
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