[7] Notably, strictly anaerobic methanotrophs may also harbour methane monooxygenases, although there are critical mismatches in the gene which prevent common methanotroph-seeking primers from matching.

[8] Methanotrophic bacteria play an essential role of cycling carbon through anaerobic sediments.

The chemistry behind the cycling takes a chemically inert hydrocarbon, methane, and converts it to a more active species, methanol.

Other hydrocarbons are oxidized by MMOs, so a new hydroxylation catalyst based on the understanding of MMO systems could possibly make a more efficient use of the world supply of natural gas.

[9] This is a classic monooxygenase reaction in which two reducing equivalents from NAD(P)H are utilized to split the O-O bond of O2.

The best characterized forms of soluble MMO contains three protein components: hydroxylase, the β unit, and the reductase.

In addition, there is a wide canyon running along the dimer interface with an opening in the center of the molecule.

[10] The two irons are at this point oxidized to FeIV and have changed from low-spin ferromagnetic to high-spin antiferromagnetic.

The nonradical mechanism implies a concerted pathway, occurring via a four-center transition state and leading to a “hydrido-alkyl-Q” compound.

On the other hand, it can start with a 2e- reduction process of bridging the O1 atom to give a water molecule, followed by elimination of the alcohol and regeneration of the enzyme.

In addition, it is possible that there is a concerted mechanism whereby the elimination of the methanol occurs spontaneously with 2e- reduction of the bridging O1 center and regeneration of the catalyst.