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A tale of two methane monooxygenases

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Abstract

Methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO). Understanding the reaction mechanisms of these enzymes is of fundamental importance to biologists and chemists, and is also relevant to the development of new biocatalysts. The sMMO catalytic cycle has been elucidated in detail, including O2 activation intermediates and the nature of the methane-oxidizing species. By contrast, many aspects of pMMO catalysis remain unclear, most notably the nuclearity and molecular details of the copper active site. Here, we review the current state of knowledge for both enzymes, and consider pMMO O2 activation intermediates suggested by computational and synthetic studies in the context of existing biochemical data. Further work is needed on all fronts, with the ultimate goal of understanding how these two remarkable enzymes catalyze a reaction not readily achieved by any other metalloenzyme or biomimetic compound.

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Abbreviations

AMO:

Ammonia monooxygenase

BMM:

Bacterial multicomponent monooxygenase

DβH:

Dopamine β-hydroxylase

EPR:

Electron paramagnetic resonance

EXAFS:

Extended X-ray absorption fine structure

HMO:

Hydrocarbon monooxygenase

MDH:

Methanol dehydrogenase

MMO:

Methane monooxygenase

MMOB:

sMMO regulatory protein

MMOH:

sMMO hydroxylase

MMOHox :

MMOH with a diiron(III) site

MMOHred :

MMOH with a diiron(II) site

MMOR:

sMMO reductase

NDH-2:

Type 2 NADH:quinone oxidoreductase

PHM:

Peptidylglycine α-hydroxylating monooxygenase

pMMO:

Particulate MMO

sMMO:

Soluble MMO

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Acknowledgements

Work in the Rosenzweig laboratory on biological methane oxidation is supported by National Institutes of Health Grant GM118035 (A. C. R.). M. O. R. was supported in part by National Institutes of Health Grant 5T32GM008382.

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  1. Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL, 60208, USA

    Matthew O. Ross & Amy C. Rosenzweig

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  1. Matthew O. Ross
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Correspondence to Amy C. Rosenzweig.

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Ross, M.O., Rosenzweig, A.C. A tale of two methane monooxygenases. J Biol Inorg Chem 22, 307–319 (2017). https://doi.org/10.1007/s00775-016-1419-y

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