ABSTRACT
Methane hydroxylase (MH) from the obligate methane assimilating culture of Methylococcus thermophilus catalyses oxygenation of both CH4+ and NH4+; therefore, we studied the specificity of enzyme systems catalysing the subsequent oxidation of compounds produced upon the oxygenation of these substrates (CH3OH and NH2OH). CH3OH and NH2OH were shown to be oxidized by different enzymes, viz. methanol dehydrogenase (MD) and hydroxylamine oxidase (HO), respectively. Similar to MH, MD is characterized by the absence of strict substrate specificity, and catalyses oxidation of primary alcohols other than methanol, rather than hydroxylamine. HO catalyses oxidation of hydroxylamine rather than methanol and possesses the activity of hydroxylamine:cytochrome c oxidoreductase. The constitutive character of HO from the methane assimilating bacteria and the substrate specificity of the enzyme suggest that a lithotrophic pathway for producing energy operates in these bacteria. The HO of Methylococcus thermophilus is similar in certain properties to the HO of the nitrifying bacterium Nitrosomonas europaea.
