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Title: Metals and Methanotrophy

Abstract

Aerobic methanotrophs have long been known to play a critical role in the global carbon cycle, being capable of converting methane to biomass and carbon dioxide. Interestingly, these microbes exhibit great sensitivity to copper and rare-earth elements, with the expression of key genes involved in the central pathway of methane oxidation controlled by the availability of these metals. That is, these microbes have a “copper switch” that controls the expression of alternative methane monooxygenases and a “rare-earth element switch” that controls the expression of alternative methanol dehydrogenases. Additionally, it has been recently shown that some methanotrophs can detoxify inorganic mercury and demethylate methylmercury; this finding is remarkable, as the canonical organomercurial lyase does not exist in these methanotrophs, implying that a novel mechanism is involved in methylmercury demethylation. Here, we review recent findings on methanotrophic interactions with metals, with a particular focus on these metal switches and the mechanisms used by methanotrophs to bind and sequester metals.

Authors:
 [1];  [2];  [1];  [3];  [4]
  1. Univ. of Michigan, Ann Arbor, MI (United States)
  2. Iowa State Univ., Ames, IA (United States)
  3. Korea Advanced Inst. Science and Technology (KAIST), Daejeon (South Korea)
  4. Univ. of Illinois, Urbana-Champaign, IL (United States)
Publication Date:
Research Org.:
Univ. of Michigan, Ann Arbor, MI (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Science Foundation (NSF)
OSTI Identifier:
1503609
Grant/Contract Number:  
SC0018059
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Applied and Environmental Microbiology
Additional Journal Information:
Journal Volume: 84; Journal Issue: 6; Journal ID: ISSN 0099-2240
Publisher:
American Society for Microbiology
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 36 MATERIALS SCIENCE; methanotrophy; methanobactin; copper; mercury; rare-earth elements

Citation Formats

Semrau, Jeremy D., DiSpirito, Alan A., Gu, Wenyu, Yoon, Sukhwan, and Cann, Isaac. Metals and Methanotrophy. United States: N. p., 2018. Web. doi:10.1128/aem.02289-17.
Semrau, Jeremy D., DiSpirito, Alan A., Gu, Wenyu, Yoon, Sukhwan, & Cann, Isaac. Metals and Methanotrophy. United States. doi:10.1128/aem.02289-17.
Semrau, Jeremy D., DiSpirito, Alan A., Gu, Wenyu, Yoon, Sukhwan, and Cann, Isaac. Fri . "Metals and Methanotrophy". United States. doi:10.1128/aem.02289-17. https://www.osti.gov/servlets/purl/1503609.
@article{osti_1503609,
title = {Metals and Methanotrophy},
author = {Semrau, Jeremy D. and DiSpirito, Alan A. and Gu, Wenyu and Yoon, Sukhwan and Cann, Isaac},
abstractNote = {Aerobic methanotrophs have long been known to play a critical role in the global carbon cycle, being capable of converting methane to biomass and carbon dioxide. Interestingly, these microbes exhibit great sensitivity to copper and rare-earth elements, with the expression of key genes involved in the central pathway of methane oxidation controlled by the availability of these metals. That is, these microbes have a “copper switch” that controls the expression of alternative methane monooxygenases and a “rare-earth element switch” that controls the expression of alternative methanol dehydrogenases. Additionally, it has been recently shown that some methanotrophs can detoxify inorganic mercury and demethylate methylmercury; this finding is remarkable, as the canonical organomercurial lyase does not exist in these methanotrophs, implying that a novel mechanism is involved in methylmercury demethylation. Here, we review recent findings on methanotrophic interactions with metals, with a particular focus on these metal switches and the mechanisms used by methanotrophs to bind and sequester metals.},
doi = {10.1128/aem.02289-17},
journal = {Applied and Environmental Microbiology},
issn = {0099-2240},
number = 6,
volume = 84,
place = {United States},
year = {2018},
month = {1}
}

Journal Article:
Free Publicly Available Full Text
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Cited by: 16 works
Citation information provided by
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Figures / Tables:

FIG 1 FIG 1: Phylogenetic distribution of aerobic methanotrophic genera. 16S rRNA sequence alignment was generated using the SILVA aligner (164) and used to construct a maximum likelihood tree based on the Tamura-Nei model in MEGA7 (165). For the sake of brevity, methanotrophic species are not listed. For a thorough list/description ofmore » validated aerobic methanotrophic species, the reader is directed to reference 6. It should be noted that to date, no type strains have been isolated/purified from the Clonothrix, Crenothrix, or Methylomirabilis genus.« less

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Rare earth elements in soil and plant systems - A review
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Highly efficient methane biocatalysis revealed in a methanotrophic bacterium
journal, December 2013

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The relationship between protein structure and function: a comprehensive survey with application to the yeast genome
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Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases
journal, December 2015

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Oxidation of methane by a biological dicopper centre
journal, April 2010

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PQQ-dependent methanol dehydrogenases: rare-earth elements make a difference
journal, May 2014

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The Surface-Associated and Secreted MopE Protein of Methylococcus capsulatus (Bath) Responds to Changes in the Concentration of Copper in the Growth Medium
journal, April 2003


Environmental, genomic and taxonomic perspectives on methanotrophic Verrucomicrobia : Perspectives on methanotrophic
journal, March 2009


The TIM-barrel fold: a versatile framework for efficient enzymes
journal, March 2001


Methylmercury uptake and degradation by methanotrophs
journal, May 2017


Ore Leaching by Bacteria
journal, October 1980


Expanding the Verrucomicrobial Methanotrophic World: Description of Three Novel Species of Methylacidimicrobium gen. nov.
journal, August 2014

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Nitrate leaching in an Andisol treated with different types of fertilizers
journal, March 2003


Copper and cerium-regulated gene expression in Methylosinus trichosporium OB3b
journal, October 2017


Molecular structure and gene analysis of Ce3+-induced methanol dehydrogenase of Bradyrhizobium sp. MAFF211645
journal, June 2011

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Taxonomic Characterization of New Alkaliphilic and Alkalitolerant Methanotrophs from Soda Lakes of the Southeastern Transbaikal Region and description of Methylomicrobium buryatense sp.nov.
journal, January 2001

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The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
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Structural and Mechanistic Insights into Methane Oxidation by Particulate Methane Monooxygenase
journal, July 2007

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MauG: a di-heme enzyme required for methylamine dehydrogenase maturation
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Uptake and effect of rare earth elements on gene expression in Methylosinus trichosporium OB3b
journal, May 2016

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Mechanisms of siderophore sorption to smectite and siderophore-enhanced release of structural Fe3+
journal, July 2008

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Stimulation of Methanotrophic Growth in Cocultures by Cobalamin Excreted by Rhizobia
journal, October 2011

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Evidence for the transport of zinc(II) ions via the Pit inorganic phosphate transport system in Escherichia coli
journal, March 2000


MEGA7: Molecular Evolutionary Genetics Analysis Version 7.0 for Bigger Datasets
journal, March 2016

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The quinoprotein dehydrogenases for methanol and glucose
journal, August 2004


Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
journal, January 2005

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Distribution of Methanotrophs in the Phyllosphere
journal, August 2012

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Copper complexation of methanobactin isolated from Methylosinus trichosporium OB3b: pH-dependent speciation and modeling
journal, November 2012


The structure of bacterial quinoprotein dehydrogenases
journal, January 1992


Lanthanide-Dependent Regulation of Methanol Oxidation Systems in Methylobacterium extorquens AM1 and Their Contribution to Methanol Growth
journal, February 2016

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Pseudomonas stutzeri N2O reductase contains CuA-type sites.
journal, June 1989

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Functional investigation of methanol dehydrogenase-like protein XoxF in Methylobacterium extorquens AM1
journal, May 2010


Methanobactin from Methylosinus trichosporium OB3b inhibits N2O reduction in denitrifiers
journal, January 2018


    Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.