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Title: Crystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain M

Abstract

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Previous biochemical and structural studies of pMMO have focused on preparations from Methylococcus capsulatus (Bath) and Methylosinus trichosporium OB3b. A pMMO from a third organism, Methylocystis species strain M, has been isolated and characterized. Both membrane-bound and solubilized Methylocystis sp. strain M pMMO contain {approx}2 copper ions per 100 kDa protomer and exhibit copper-dependent propylene epoxidation activity. Spectroscopic data indicate that Methylocystis sp. strain M pMMO contains a mixture of Cu{sup I} and Cu{sup II}, of which the latter exhibits two distinct type 2 Cu{sup II} electron paramagnetic resonance (EPR) signals. Extended X-ray absorption fine structure (EXAFS) data are best fit with a mixture of Cu-O/N and Cu-Cu ligand environments with a Cu-Cu interaction at 2.52-2.64 {angstrom}. The crystal structure of Methylocystis sp. strain M pMMO was determined to 2.68 {angstrom} resolution and is the best quality pMMO structure obtained to date. It provides a revised model for the pmoA and pmoC subunits and has led to an improved model of M. capsulatus (Bath) pMMO. In these new structures, the intramembrane zinc/copper binding site has a different coordination environment from that in previousmore » models.« less

Authors:
; ; ; ; ;  [1]
  1. WSU-MED
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1031949
Resource Type:
Journal Article
Journal Name:
Biochemistry-US
Additional Journal Information:
Journal Volume: 50; Journal Issue: (47) ; 11, 2011; Journal ID: ISSN 0006-2960
Country of Publication:
United States
Language:
ENGLISH
Subject:
03 NATURAL GAS; 10 SYNTHETIC FUELS; ABSORPTION; COPPER IONS; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; FINE STRUCTURE; MEMBRANES; METHANE; METHANOL; METHANOTROPHIC BACTERIA; MIXTURES; PARTICULATES; PROPYLENE; RESOLUTION; STRAINS

Citation Formats

Smith, Stephen M, Rawat, Swati, Telser, Joshua, Hoffman, Brian M, Stemmler, Timothy L, Rosenzweig, Amy C, and NWU). Crystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain M. United States: N. p., 2012. Web. doi:10.1021/bi200801z.
Smith, Stephen M, Rawat, Swati, Telser, Joshua, Hoffman, Brian M, Stemmler, Timothy L, Rosenzweig, Amy C, & NWU). Crystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain M. United States. https://doi.org/10.1021/bi200801z
Smith, Stephen M, Rawat, Swati, Telser, Joshua, Hoffman, Brian M, Stemmler, Timothy L, Rosenzweig, Amy C, and NWU). Wed . "Crystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain M". United States. https://doi.org/10.1021/bi200801z.
@article{osti_1031949,
title = {Crystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain M},
author = {Smith, Stephen M and Rawat, Swati and Telser, Joshua and Hoffman, Brian M and Stemmler, Timothy L and Rosenzweig, Amy C and NWU)},
abstractNote = {Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Previous biochemical and structural studies of pMMO have focused on preparations from Methylococcus capsulatus (Bath) and Methylosinus trichosporium OB3b. A pMMO from a third organism, Methylocystis species strain M, has been isolated and characterized. Both membrane-bound and solubilized Methylocystis sp. strain M pMMO contain {approx}2 copper ions per 100 kDa protomer and exhibit copper-dependent propylene epoxidation activity. Spectroscopic data indicate that Methylocystis sp. strain M pMMO contains a mixture of Cu{sup I} and Cu{sup II}, of which the latter exhibits two distinct type 2 Cu{sup II} electron paramagnetic resonance (EPR) signals. Extended X-ray absorption fine structure (EXAFS) data are best fit with a mixture of Cu-O/N and Cu-Cu ligand environments with a Cu-Cu interaction at 2.52-2.64 {angstrom}. The crystal structure of Methylocystis sp. strain M pMMO was determined to 2.68 {angstrom} resolution and is the best quality pMMO structure obtained to date. It provides a revised model for the pmoA and pmoC subunits and has led to an improved model of M. capsulatus (Bath) pMMO. In these new structures, the intramembrane zinc/copper binding site has a different coordination environment from that in previous models.},
doi = {10.1021/bi200801z},
url = {https://www.osti.gov/biblio/1031949}, journal = {Biochemistry-US},
issn = {0006-2960},
number = (47) ; 11, 2011,
volume = 50,
place = {United States},
year = {2012},
month = {2}
}