Methanotrophs, monooxygenases monooxygenase

A few of the reactions carried out by the monooxygenase system of methanotrophic bacteria are summarized in Figure 2.9, and it is on account of this that methylotrophs have received attention for their technological potential (Lidstrom and Stirling 1990). An equally wide metabolic potential has also been demonstrated for cyclohexane monooxygenase, which has been shown to accomplish two broad types of reaction one in which formally nucleophilic oxygen reacts with the substrate, and... 

FIGURE 2.9 Reactions mediated by the monooxygenase system of methanotrophic bacteria. 

Methane monooxygenase may exist in either soluble (sMMO) or particulate (pMMO) forms. These display different substrate ranges and different rates of transformation rates, and most methanotrophs express only the latter form of the enzyme (Hanson and Hanson 1996). The particulate form of methane monooxygenase contains copper, or both copper... 

Fox BG, Wa Froland, JE Dege, JD Lipscomb (1989) Methane monooxygenase from Methylosinus trichospo-rium OB3b. Purification and properties of a three-component system with a high specific activity from a type II methanotroph. J Biol Chem 264 10023-10033. 

Methanotrophs rely on the enzymatic system methane monooxygenase (MMO) to catalyze the first step in the metabolism of methane, shown in Eq. (1) (1, 14). 

In some cases, microorganisms can transform a contaminant, but they are not able to use this compound as a source of energy or carbon. This biotransformation is often called co-metabolism. In co-metabolism, the transformation of the compound is an incidental reaction catalyzed by enzymes, which are involved in the normal microbial metabolism.33 A well-known example of co-metabolism is the degradation of (TCE) by methanotrophic bacteria, a group of bacteria that use methane as their source of carbon and energy. When metabolizing methane, methanotrophs produce the enzyme methane monooxygenase, which catalyzes the oxidation of TCE and other chlorinated aliphatics under aerobic conditions.34 In addition to methane, toluene and phenol have been used as primary substrates to stimulate the aerobic co-metabolism of chlorinated solvents. 

Oremland et al. [136] subsequently demonstrated that methane-oxidizing bacteria also had the capacity to co-oxidize methyl bromide by methane monooxygenase produced during the oxidation of methane to methanol. They also showed that methanotrophic soils that had a high capacity to oxidize methane degraded14C-labeled methyl bromide to 14C02. 

Two types of methane monooxygenases have been studied (1) soluble methane monooxygenase (sMMO) and (2) particulate (membrane-bound) methane monooxygenase (pMMO). The well-studied sMMO is produced by methanotrophs under copper-limiting conditions. All methanotrophs produce pMMO—found in intracytoplasmic membranes— but it is the less well-studied enzyme. 

Koh, S.-C., J. P. Bowman, and G. S. Sayler, Soluble methane monooxygenase production and trichloroethylene degradation by a type I methanotroph, Methylomonas methanica 68-1 , Appl. Environ. Microbiol., 59,960-967 (1993). 

Non-heme iron-containing monooxygenases are able to catalyze the oxidation of hydrocarbons to the corresponding hydrocarbon alcohols and have been found in methanotrophic bacteria [58]. 

Some preparations of iron exchanged into zeolite H-MFI by vapor-phase FeCL are known to be active and selective catalysts for the reduction of NO, with hydrocarbons or ammonia in the presence of excess oxygen and water vapor (45,46). The active centers in Fe/MFI are assumed to be binuclear, oxygen-bridged iron complexes, as follows from H2-TPR, CO-TPR, and ESR data (45,47) and EXAFS and XANES results (48,49). These complexes are structurally similar to the binuclear iron centers in methane monooxygenase enzymes that are employed by methanotrophic bacteria in utilization of methane as their primary energy source (50). It is believed that molecular oxygen reacts with these centers to form peroxide as the initial step in this chemistry (50). 

Fox, B. G., and Lipscomb, J. D., 1988, Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph, Biochem. Biophys. Res. Commun. 154 165nl70. 

McDonald I. R. and Murrell J. C. (1997) The particulate methane monooxygenase gene pmoA and its use as a functional gene probe for methanotrophs. FEMS Microbiol. Lett. 156, 205-210. 

Figure 10 Theoretical (a) and practical (b) representation of QSARs. Panel b describes a QSAR for the methanotrophic oxidation (activity of methane monooxygenase) of 6>r /i6>(Ci2)-substituted biphenyls. The structural backbone was biphenyl, and the substituents considered included all halogens, methyl-, methoxy-, hydroxyl-, nitro-, and amino-moieties (Lindner et al, 2003). The molecular descriptors used in (b) are (charge on the ortho-csubon), (Taft s steric parameter), and log ow...

---