scholarly journals Revisiting the Mechanism of Dioxygen Activation in Soluble Methane Monooxygenase fromM. capsulatus(Bath): Evidence for a Multi-Step, Proton-Dependent Reaction Pathway

Biochemistry ◽  
2009 ◽  
Vol 48 (51) ◽  
pp. 12145-12158 ◽  
Author(s):  
Christine E. Tinberg ◽  
Stephen J. Lippard
Keyword(s):  
Reaction Pathway ◽  
Methane Monooxygenase ◽  
Dioxygen Activation ◽  
Soluble Methane Monooxygenase

scholarly journals Dioxygen Activation in Soluble Methane Monooxygenase

2011 ◽  
Vol 44 (4) ◽  
pp. 280-288 ◽  
Author(s):  
Christine E. Tinberg ◽  
Stephen J. Lippard
Keyword(s):  
Methane Monooxygenase ◽  
Dioxygen Activation ◽  
Soluble Methane Monooxygenase

ChemInform Abstract: Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins

ChemInform ◽  
2010 ◽  
Vol 32 (46) ◽  
pp. no-no
Author(s):  
Maarten Merkx ◽  
Daniel A. Kopp ◽  
Matthew H. Sazinsky ◽  
Jessica L. Blazyk ◽  
Jens Mueller ◽  
...  
Keyword(s):  
Methane Monooxygenase ◽  
Dioxygen Activation ◽  
Soluble Methane Monooxygenase

Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins

2001 ◽  
Vol 40 (15) ◽  
pp. 2782-2807 ◽  
Author(s):  
Maarten Merkx ◽  
Daniel A. Kopp ◽  
Matthew H. Sazinsky ◽  
Jessica L. Blazyk ◽  
Jens Müller ◽  
...  
Keyword(s):  
Methane Monooxygenase ◽  
Dioxygen Activation ◽  
Soluble Methane Monooxygenase

Soluble Methane Monooxygenase Component Interactions Monitored by 19F NMR

Biochemistry ◽  
2021 ◽  
Author(s):  
Jason C. Jones ◽  
Rahul Banerjee ◽  
Ke Shi ◽  
Manny M. Semonis ◽  
Hideki Aihara ◽  
...  
Keyword(s):  
Methane Monooxygenase ◽  
19F Nmr ◽  
Soluble Methane Monooxygenase

scholarly journals Methanobactin from Methylocystis sp. Strain SB2 Affects Gene Expression and Methane Monooxygenase Activity in Methylosinus trichosporium OB3b

2015 ◽  
Vol 81 (7) ◽  
pp. 2466-2473 ◽  
Author(s):  
Muhammad Farhan Ul-Haque ◽  
Bhagyalakshmi Kalidass ◽  
Alexey Vorobev ◽  
Bipin S. Baral ◽  
Alan A. DiSpirito ◽  
...  
Keyword(s):  
Gene Expression ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Methylosinus Trichosporium Ob3b ◽  
Methylosinus Trichosporium ◽  
Monooxygenase Activity ◽  
Content Type ◽  
Soluble Methane Monooxygenase ◽  
A Subunit ◽  
Membrane Bound

ABSTRACTMethanotrophs can express a cytoplasmic (soluble) methane monooxygenase (sMMO) or membrane-bound (particulate) methane monooxygenase (pMMO). Expression of these MMOs is strongly regulated by the availability of copper. Many methanotrophs have been found to synthesize a novel compound, methanobactin (Mb), that is responsible for the uptake of copper, and methanobactin produced byMethylosinus trichosporiumOB3b plays a key role in controlling expression of MMO genes in this strain. As all known forms of methanobactin are structurally similar, it was hypothesized that methanobactin from one methanotroph may alter gene expression in another. WhenMethylosinus trichosporiumOB3b was grown in the presence of 1 μM CuCl2, expression ofmmoX, encoding a subunit of the hydroxylase component of sMMO, was very low.mmoXexpression increased, however, when methanobactin fromMethylocystissp. strain SB2 (SB2-Mb) was added, as did whole-cell sMMO activity, but there was no significant change in the amount of copper associated withM. trichosporiumOB3b. IfM. trichosporiumOB3b was grown in the absence of CuCl2, themmoXexpression level was high but decreased by several orders of magnitude if copper prebound to SB2-Mb (Cu-SB2-Mb) was added, and biomass-associated copper was increased. Exposure ofMethylosinus trichosporiumOB3b to SB2-Mb had no effect on expression ofmbnA, encoding the polypeptide precursor of methanobactin in either the presence or absence of CuCl2.mbnAexpression, however, was reduced when Cu-SB2-Mb was added in both the absence and presence of CuCl2. These data suggest that methanobactin acts as a general signaling molecule in methanotrophs and that methanobactin “piracy” may be commonplace.

scholarly journals Competition between Metals for Binding to Methanobactin Enables Expression of Soluble Methane Monooxygenase in the Presence of Copper

2014 ◽  
Vol 81 (3) ◽  
pp. 1024-1031 ◽  
Author(s):  
Bhagyalakshmi Kalidass ◽  
Muhammad Farhan Ul-Haque ◽  
Bipin S. Baral ◽  
Alan A. DiSpirito ◽  
Jeremy D. Semrau
Keyword(s):  
Methane Monooxygenase ◽  
High Specificity ◽  
Copper Uptake ◽  
Content Type ◽  
Soluble Methane Monooxygenase ◽  
Sds Page ◽  
Genes Encoding ◽  
Key Factor ◽  
Membrane Bound

ABSTRACTIt is well known that copper is a key factor regulating expression of the two forms of methane monooxygenase found in proteobacterial methanotrophs. Of these forms, the cytoplasmic, or soluble, methane monooxygenase (sMMO) is expressed only at low copper concentrations. The membrane-bound, or particulate, methane monooxygenase (pMMO) is constitutively expressed with respect to copper, and such expression increases with increasing copper. Recent findings have shown that copper uptake is mediated by a modified polypeptide, or chalkophore, termed methanobactin. Although methanobactin has high specificity for copper, it can bind other metals, e.g., gold. Here we show that inMethylosinus trichosporiumOB3b, sMMO is expressed and active in the presence of copper if gold is also simultaneously present. Such expression appears to be due to gold binding to methanobactin produced byM. trichosporiumOB3b, thereby limiting copper uptake. Such expression and activity, however, was significantly reduced if methanobactin preloaded with copper was also added. Further, quantitative reverse transcriptase PCR (RT-qPCR) of transcripts of genes encoding polypeptides of both forms of MMO and SDS-PAGE results indicate that both sMMO and pMMO can be expressed when copper and gold are present, as gold effectively competes with copper for binding to methanobactin. Such findings suggest that under certain geochemical conditions, both forms of MMO may be expressed and activein situ. Finally, these findings also suggest strategies whereby field sites can be manipulated to enhance sMMO expression, i.e., through the addition of a metal that can compete with copper for binding to methanobactin.

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