Interaction of dichloromethane (methylene chloride) with the nitrous oxide reductase from Wolinella succinogenes.

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.