The study, "Particulate methane monooxygenase
contains only mononuclear copper centers," was supported by the National Institutes of Health (award numbers GM118035, GM111097 and 5T32GM008382) and the National Science Foundation (award number 1534743).
Methane monooxygenase (MMO) is such a fascinating enzyme that can efficiently catalyze ethylene to ethylene epoxide with high region specificity and stereoselectivity [8, 9].
Abbreviations MMO: Methane monooxygenase NADH: Nicotinamide adenine dinucleotide NMS: Nitrate mineral salts medium NAD: Nicotinamide adenine dinucleotide MMOH: Methane monooxygenase hydroxylase.
Other proteins and topics covered include radical S-adenosyl-1-methionine (SAM) enzymes, density functional theory (DFT) modeling of active sites, methane monooxygenase
catalysis, electrochemistry at metalloenzymes, iron uptake in ferritin, multistep electron flow, and ligand binding models.
The effect of nitrogenous substrates on methane oxidation has been the most investigated but no consistent patterns could be generalized, and hence the interactions between the nitrogen and methane cycle are far more complicated than previously appreciated (Bodelier, 2011).The particulate methane monooxygenase (pmoA) genes of MOB and the ammonia monooxygenase (amoA) genes of AOB are evolutionarily related to each other (Holmes et al., 1995).
Evidence that particulate methane monooxygenase and ammoniamonooxygenase may be evolutionarily related.
Polymerase chain reaction analysis revealed soluble methane monooxygenase genes in methanotrophic enrichments, and 16S rRNA analysis identified Methylocystis parvus with 98% similarity, further indicating the presence of a type II methanotroph.
Optimization of trichloroethylene oxidation by methanotrophs and the use of a colorimetric assay to detect soluble methane monooxygenase activity.
"Following the isolation of Methylobacterium extorquens by the Sector several years ago, this microorganism is now being developed as a prokaryotic in-house expression system." Miguez adds, "the gene cluster cloning for an enzyme called soluble methane monooxygenase
(sMMO) is being cloned into Methylobacterium extorquens.
Extensive published research on enzyme active site structures such as those found in hemerythrin, ribonucleotide reductase, methane monooxygenase
and many other enzymes reveals the presence of binuclear metallic cores, many of which are carboxylate-bridged (refs.