Studies by e.p.r. spectroscopy of carbon monoxide oxidases from Pseudomonas carboxydovorans and Pseudomonas carboxydohydrogena.
E.p.r. spectra were obtained at 8-120 K for carbon monoxide oxidases isolated from the carboxydotrophic bacteria Pseudomonas carboxydovorans and Pseudomonas carboxydohydrogena. Spectra from the two enzymes are extremely similar to one another. Under appropriate conditions each enzyme shows signals from Mo(V) atoms in two different chemical environments, as well as showing signals from two distinct iron-sulphur centres, presumed to be [2Fe-2S] clusters, and weak FADH X free-radical signals. Parameters of most of the signals were measured, and they show considerable similarities to those of the corresponding signals from xanthine oxidase and related enzymes. Though the signals from carbon monoxide oxidases appear and disappear under reducing and oxidizing conditions, we have so far failed to demonstrate the kinetic competence of any of them. It seems likely that this was due to the presence in the enzyme preparation examined of high amounts of desulpho carbon monoxide oxidase together with another non-functional form of the enzyme giving a stable 'Resting' Mo(V) e.p.r. signal.
D000445:Aldehyde Oxidoreductases; D004227:Dithionite; D004578:Electron Spin Resonance Spectroscopy; D007501:Iron; D011549:Pseudomonas / Q000201:enzymology*; D013455:Sulfur
D004227:Dithionite; D013455:Sulfur; D007501:Iron; D000445:Aldehyde Oxidoreductases; C033598:carbon monoxide-methylene blue oxidoreductase