Molybdenum-free nitrate reductases from vanadate-reducing bacteria.
Two catalytically distinct molybdenum-free dissimilatory nitrate reductases, a soluble periplasmic and a membrane-bound one, were isolated from the vanadate-reducing facultatively anaerobic bacterium Pseudomonas isachenkovii and purified to electrophoretic homogeneity. The enzymes did not contain molybdenum, the periplasmic enzyme contained vanadium, whereas the membrane-bound enzyme was vanadium-free. Both nitrate reductases lacked molybdenum cofactor. This fact was proved by reconstitution of the apoprotein of the nitrate reductase of Neurospora crassa nit-1 mutant. This is the first demonstration of molybdenum-free and molybdenum cofactor-free nitrate reductases.
Antipov
A N
AN
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.
Lyalikova
N N
NN
Khijniak
T V
TV
L'vov
N P
NP
D004577:Electron Probe Microanalysis; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry / Q000379:methods; D008982:Molybdenum / Q000737:chemistry*; D009565:Nitrate Reductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D014638:Vanadates / Q000737:chemistry / Q000378:metabolism*
D014638:Vanadates; D008982:Molybdenum; D009565:Nitrate Reductases