Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens.
A new procedure for isolation of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens increasing significantly the yield of the purified enzyme is presented. The enzyme is isolated from the soluble fraction of the cell extract as a hexamer, as shown by gel filtration chromatography and small angle X-ray scattering analysis. Thermostability of the hexameric form of the nitrite reductase is characterized in terms of thermoinactivation and thermodenaturation.
Tikhonova
T V
TV
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. ttikhonova@inbi.ras.ru
Slutskaya
E S
ES
Filimonenkov
A A
AA
Boyko
K M
KM
Kleimenov
S Yu
SY
Konarev
P V
PV
Polyakov
K M
KM
Svergun
D I
DI
Trofimov
A A
AA
Khomenkov
V G
VG
Zvyagilskaya
R A
RA
Popov
V O
VO
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D045263:Cytochromes a1 / Q000737:chemistry* / Q000302:isolation & purification*; D003575:Cytochromes c1 / Q000737:chemistry* / Q000302:isolation & purification*; D042001:Ectothiorhodospiraceae / Q000201:enzymology*; D004795:Enzyme Stability; D009565:Nitrate Reductases / Q000737:chemistry* / Q000302:isolation & purification*; D053838:Scattering, Small Angle; D013696:Temperature; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D045263:Cytochromes a1; D003575:Cytochromes c1; D009565:Nitrate Reductases; C054690:nitrate reductase (cytochrome)