Abstract
Nitrous oxide reductase from Wolinella succinogenes was tested for benzyl viologen cation (BV+)-chlorinated methane oxidoreductase activity, using di-, tri- and tetra-chloromethanes, and for the inhibition of BV+-N2O oxidoreductase activity by these chloromethanes. No BV+-chlorinated methane oxidoreductase activity was detected. Any such activity, if it exists, must be less than 0.1% of the BV+-N2O oxidoreductase activity of the enzyme. Inhibition of the BV+-N2O oxidoreductase activity by dichloromethane was detected and was apparently reversible and non-competitive, as is the case with the small metal-ligand type inhibitors of the enzyme (e.g. acettlene, azide, cyanide and carbon monoxide). Trichloromethane was a weaker inhibitor and inhibition was not detected with tetrachloromethane.
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Zhang, C., Hollocher, T.C. Interaction of dichloromethane (methylene chloride) with the nitrous oxide reductase from Wolinella succinogenes . World Journal of Microbiology and Biotechnology 9, 479–482 (1993). https://doi.org/10.1007/BF00328037
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DOI: https://doi.org/10.1007/BF00328037