Methane monooxygenase reactions

Single Species at Specified pH ill 9.3 Methane Monooxygenase Reaction... 

Table 9.3 Standard Transformed Gibbs Energies (in kJ moE ) of Reactions and Standard Apparent Reduction Potentials (in volts) at 289.15 K, 1 bar, pH 7, and Ionic Strength 0.25 M for Reactions Involved in the Methane Monooxygenase Reaction...

The methane monooxygenase reaction can, in principle, be carried out in two other ways by the enzyme complex that catalyzes it It can be carried out in three half-reactions at three catalytic sites as follows ... 

The third largest class of enzymes is the oxidoreductases, which transfer electrons. Oxidoreductase reactions are different from other reactions in that they can be divided into two or more half reactions. Usually there are only two half reactions, but the methane monooxygenase reaction can be divided into three "half reactions." Each chemical half reaction makes an independent contribution to the equilibrium constant E for a chemical redox reaction. For chemical reactions the standard reduction potentials ° can be determined for half reactions by using electrochemical cells, and these measurements have provided most of the information on standard chemical thermodynamic properties of ions. This research has been restricted to rather simple reactions for which electrode reactions are reversible on platinized platinum or other metal electrodes. 

FIGURE 7.1 Examples of the reactions catalyzed by methane monooxygenase. 

Basch, H., Mogi, K., Musaev, D. G., Morokuma, K., 1999, Mechanism of the Methane —> Methanol Conversion Reaction Catalyzed by Methane Monooxygenase A Density Functional Study , J. Am. Chem. Soc., 121, 7249. 

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. 

Metalloenzymes with non-heme di-iron centers in which the two irons are bridged by an oxide (or a hydroxide) and carboxylate ligands (glutamate or aspartate) constitute an important class of enzymes. Two of these enzymes, methane monooxygenase (MMO) and ribonucleotide reductase (RNR) have very similar di-iron active sites, located in the subunits MMOH and R2 respectively. Despite their structural similarity, these metal centers catalyze very different chemical reactions. We have studied the enzymatic mechanisms of these enzymes to understand what determines their catalytic activity [24, 25, 39-41]. 

Itoh et al. used Cu yd-diketiminato complexes with general formula 4, and their reactivity has been described as a functional model for pMMO (particulate methane monooxygenase). Initially, the Hgands were reacted with both Cu and Cu precursors, with a variety of species formed, depending on the specific conditions employed [111, 112]. It was then shown that both Cu and Cu complexes ultimately led to bis(/z-oxo)(Cu )2 species upon reaction with O2 and H2O2, respectively. Use of these Cu complexes as the pre-catalysts for the oxidation of alkanes (cyclohexane and adamantane) in the presence of H2O2 resulted in low yields ( 20%). 

Scheme 2.6 Examples of reactions catalyzed byenzymesthat carry a dinudear iron active site (a) hydroxylation of methane by soluble methane monooxygenase (sMMO) [7] (b) reduction of ribonucleotides by class I ribonucleotide reductase (RNR)...

The curve of 02 accumulation shows that short contact times, at which the methane oxidation rate is low, are enough for complete H202 dissociation. However, as observed from shapes of 02 and CH3OH accumulation curves, methanol yield increases synchronously with 02 yield decrease, and from the moment r = 10.2 s both curves stabilize. Such stabilization and synchronization of catalase and monooxygenase reaction product yields is the experimental proof of their interaction, displayed by chemical conjugation. The existence of the stabilization zone of 02 and CH3OH yields is associated with full H202 dissociation. 

First two complexes with a (p.-oxo)(p-hydroxo)diiron (III) core [Fe2(0)(0H)(6TLA)2(C104)3] (I) and [Fe2(0)2(6TLA)2(C104)2] (II), were isolated and characterized (Zang et al 1995). Structure of a (-l,2-peroxo)bis(-carboxylato)diiron(m)model for the peroxo intermediate in the methane monooxygenase hydroxylase reaction cycle is presented in Fig, 6.3. 

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