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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/7047

Title: Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purification, crystallization and preliminary X-ray analysis
Authors: Coelho, Catarina
J. Gonzaléz, Pablo
Trincão, José
Carvalho, Ana L.
Najmudin, Shabir
Moura, José J. G.
Hettman, Thomas
Dieckman, Stephan
Moura, Isabel
Romão, Maria J.
Issue Date: 2007
Publisher: International Union of Crystallography
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 ° , ß = 100.7°, space group C2, and one heterodimer is present per asymmetric unit.
Description: Acta Cryst. (2007). F63, 516–519
URI: http://hdl.handle.net/10362/7047
ISSN: 1744-3091
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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