Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens.
A novel cytochrome c nitrite reductase (TvNiR) was isolated from the haloalkalophilic bacterium Thioalkalivibrio nitratireducens. The enzyme catalyses nitrite and hydroxylamine reduction, with ammonia as the only product of both reactions. It consists of 525 amino-acid residues and contains eight haems c. TvNiR crystals were grown by the hanging-drop vapour-diffusion technique. The crystals display cubic symmetry and belong to space group P2(1)3, with unit-cell parameter a = 194 A. A native data set was obtained to 1.5 A resolution. The structure was solved by the SAD technique using the data collected at the Fe absorption peak wavelength.
Boyko
K M
KM
A. N. Bakh Institute of Biochemistry, RAS, Moscow, Russia. boiko_konstantin@inbi.ras.ru
Polyakov
K M
KM
Tikhonova
T V
TV
Slutsky
A
A
Antipov
A N
AN
Zvyagilskaya
R A
RA
Bourenkov
G P
GP
Popov
A N
AN
Lamzin
V S
VS
Popov
V O
VO
D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D045263:Cytochromes a1 / Q000737:chemistry*; D003575:Cytochromes c1 / Q000737:chemistry*; D042001:Ectothiorhodospiraceae / Q000201:enzymology*; D006418:Heme / Q000032:analysis; D009565:Nitrate Reductases / Q000737:chemistry*
D006418:Heme; D045263:Cytochromes a1; D003575:Cytochromes c1; D009565:Nitrate Reductases; C054690:nitrate reductase (cytochrome)