Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

Lieberman, Raquel L.; Rosenzweig, Amy C.

doi:10.1038/nature03311

Cited by 594 publications

(674 citation statements)

References 44 publications

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“…Thus, it seems that the formation of the chemical adduct at K196 is perhaps not an accident, as there is a thermodynamic driving force for a ketene formed at the catalytic site to find its way to this region of the protein for the acetylation reaction. We have compared the results of docking experiments between the two crystal structures of pMMO available [10,12] and the same outcomes are obtained ( Fig. 5 and Fig.…”

Section: Docking Acetylene N-alkane Substrates and Their Oxidation Pmentioning

confidence: 93%

“…10 Ribbon diagram of the polypeptide backbones associated with the three subunits: PmoA (magenta); PmoB (yellow); PmoC (green). Reproduced from reference 1.…”

Section: Scheme 1 X-ray Crystal Structure Of the Cu 3 -Pmmo Of Methymentioning

confidence: 99%

“…Crystal structures of pMMO (1YEW) [10] and (3RGB) [12] obtained from the RSCB Protein Data Bank were used for this purpose. Ions were removed and hydrogen atoms were added to the protein by the TLEAP package [24].…”

Section: Docking Experimentsmentioning

confidence: 99%

“…Highly active protein preparations consisting of the full complement of 12-15 copper ions per protein monomer have been reported [6][7][8][9]. However, crystal structure studies from different species [10][11][12] have appeared showing the trimeric architecture of the pMMO complexes, each consisting of one copy of the PmoA, PmoC, and PmoC subunits, but with just 2-3 coppers and one zinc ion per monomer. This indicates a loss of some copper ions and metal replacement during the enzyme purification and crystallization [13].…”

Section: Introductionmentioning

confidence: 99%

“…Within the transmembrane domain, there is one "zinc site" observed in the crystal structures [10][11][12] and the putative tricopper site that is proposed to be located at site D of the protein [1,16]. A dioxo-diiron cluster has also been suggested to reside in the "zinc site" [17].…”

mentioning

confidence: 99%

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Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene

Pham

Lin

Vuong

et al. 2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene, BBA -Proteins and Proteomics (2015), doi: 10.1016/j.bbapap.2015 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. experiments with two related alkynes: propyne (CH 3 CCH) and trifluoropropyne (CF 3 CCH). Finally, we discuss the implication of these findings to the location of the catalytic site in pMMO. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT

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Section: Docking Acetylene N-alkane Substrates and Their Oxidation Pmentioning

confidence: 93%

“…10 Ribbon diagram of the polypeptide backbones associated with the three subunits: PmoA (magenta); PmoB (yellow); PmoC (green). Reproduced from reference 1.…”

Section: Scheme 1 X-ray Crystal Structure Of the Cu 3 -Pmmo Of Methymentioning

confidence: 99%

Section: Docking Experimentsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene

Pham

Lin

Vuong

et al. 2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Particulate Methane Monooxygenase

Rosenzweig

2004

Handbook of Metalloproteins

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Particulate methane monooxygenase (pMMO) catalyzes the oxidation of methane to methanol in methanotrophic bacteria. The 300‐kDa pMMO enzyme is a trimeric integral membrane protein, comprising three copies each of three subunits: pmoB, pmoA, and pmoC. Purified pMMO contains both copper and iron, although some of the iron may be due to heme contamination. The copper stoichiometry ranges from 2 to 15 copper ions per 100‐kDa pMMO protomer, depending on the enzyme source. EPR spectra of whole cells, membrane‐bound, and purified pMMO consistently indicate the presence of type 2 Cu(II). According to XAS data, both Cu(I) and Cu(II) are present. EXAFS data reveal the presence of oxygen/nitrogen ligands and a short CuCu interaction at 2.5 Å that increases to 2.6 Å upon chemical reduction. Crystal structures of pMMO from two organisms have been reported. A soluble region consisting of six cupredoxin‐like β‐barrel structures is supported by 15 transmembrane helices. Three different metal centers have been detected crystallographically: a highly conserved dinuclear copper center, a nonconserved mononuclear copper center, and a site that can be occupied by zinc or copper. Although the identity of the pMMO active site remains unknown, some information regarding the mechanism has been obtained from substrate studies and computational work.

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Copper Enzymes/Models

Park¹,

Lee²,

Karlin³

2010

Encyclopedia of Catalysis

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Copper is utilized as a catalytic metal center in a variety of enzymes involved in oxidation–reduction processes. The Cu(I) and Cu(II) oxidation states are readily accessible and interconvertible under physiological conditions via oxidants (ie, O 2 ) or reducing agents such as ascorbic acid or glutathione. The important chemical transformations that these enzymes are responsible for include dioxygen processing as well as nitrogen oxide (NOx) conversions. The active site structures and catalytic mechanisms of the most well‐studied copper enzymes are described. The contributions to the understanding of enzyme function obtained from biomimetic studies using synthetic copper complexes of most relevance to the active site features have also been highlighted.

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Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

Cited by 594 publications

References 44 publications

Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene

Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene

Particulate Methane Monooxygenase

Copper Enzymes/Models

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