Evidence for an [Fe]-type hydrogenase in the parasitic protozoan Trichomonas vaginalis.
The hydrogenase of the pathogenic protozoan Trichomonas vaginalis was extracted and partially purified. The catalytic and spectroscopic properties of the enzyme indicate that it belongs to the class of [Fe]-hydrogenases, rather than the [NiFe]-hydrogenases. The hydrogenase activity was highly sensitive to carbon monoxide, 50% inhibition being attained by 1 microM CO. The EPR spectrum of the most active fractions from chromatography, after reduction by hydrogen and partial reoxidation under argon, showed an EPR spectrum at g = 2.10, 2.04, 2.00. This unusual spectrum is characteristic of the 'H-cluster', as seen in [Fe]-hydrogenases of anaerobic bacteria such as Clostridium spp.
Payne
M J
MJ
Division of Life Sciences, King's College London, UK.
Chapman
A
A
Cammack
R
R
D000818:Animals; D002248:Carbon Monoxide / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D006864:Hydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D007501:Iron / Q000737:chemistry; D014246:Trichomonas vaginalis / Q000201:enzymology*
D002248:Carbon Monoxide; D007501:Iron; D006864:Hydrogenase