Methanol Dehydrogenase, a PQQ-Containing Quinoprotein Dehydrogenase

2000 ◽  
pp. 73-117 ◽  
Author(s):  
Christopher Anthony
Keyword(s):  
Methanol Dehydrogenase

scholarly journals The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution.

1992 ◽  
Vol 267 (31) ◽  
pp. 22289-22297
Author(s):  
Z.X. Xia ◽  
W.W. Dai ◽  
J.P. Xiong ◽  
Z.P. Hao ◽  
V.L. Davidson ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Methanol Dehydrogenase ◽  
Methylotrophic Bacteria

Methanol Dehydrogenase from Nocardia SP. 239

1989 ◽  
pp. 50-53 ◽  
Author(s):  
P. W. van Ophem ◽  
J. A. Duine
Keyword(s):  
Methanol Dehydrogenase ◽  
Nocardia Sp

scholarly journals A Mutagenic Screen Identifies a TonB-Dependent Receptor Required for the Lanthanide Metal Switch in the Type I Methanotroph “Methylotuvimicrobium buryatense” 5GB1C

2019 ◽  
Vol 201 (15) ◽  
Author(s):  
Joseph D. Groom ◽  
Stephanie M. Ford ◽  
Mitchell W. Pesesky ◽  
Mary E. Lidstrom
Keyword(s):  
Metal Ion ◽  
Single Gene ◽  
Methanol Dehydrogenase ◽  
Chemical Mutagenesis ◽  
Type I ◽  
Biological Interactions ◽  
Atmospheric Methane ◽  
Metal Transporters ◽  
Lanthanide Metals ◽  
Lanthanide Metal

ABSTRACTSeveral of the metabolic enzymes in methanotrophic bacteria rely on metals for both their expression and their catalysis. The MxaFI methanol dehydrogenase enzyme complex uses calcium as a cofactor to oxidize methanol, while the alternative methanol dehydrogenase XoxF uses lanthanide metals such as lanthanum and cerium for the same function. Lanthanide metals, abundant in the earth’s crust, strongly repress the transcription ofmxaFyet activate the transcription ofxoxF. This regulatory program, called the “lanthanide switch,” is central to methylotrophic metabolism, but only some of its components are known. To uncover additional components of the lanthanide switch, we developed a chemical mutagenesis system in the type I gammaproteobacterial methanotroph “Methylotuvimicrobium buryatense” 5GB1C and designed a selection system for mutants unable to repress themxaFpromoter in the presence of lanthanum. Whole-genome resequencing for multiple lanthanide switch mutants identified several unique point mutations in a single gene encoding a TonB-dependent receptor, which we have named LanA. The LanA TonB-dependent receptor is absolutely required for the lanthanide switch and controls the expression of a small set of genes. While mutation of thelanAgene does not affect the amount of cell-associated lanthanum, it is essential for growth in the absence of the MxaF methanol dehydrogenase, suggesting that LanA is involved in lanthanum uptake to supply the XoxF methanol dehydrogenase with its critical metal ion cofactor. The discovery of this novel component of the lanthanide regulatory system highlights the complexity of this circuit and suggests that further components are likely involved.IMPORTANCELanthanide metals, or rare earth elements, are abundant in nature and used heavily in technological devices. Biological interactions with lanthanides are just beginning to be unraveled. Until very recently, microbial mechanisms of lanthanide metal interaction and uptake were unknown. The TonB-dependent receptor LanA is the first lanthanum receptor identified in a methanotroph. Sequence homology searches with known metal transporters and regulators could not be used to identify LanA or other lanthanide metal switch components, and this method for mutagenesis and selection was required to identify the receptor. This work advances the knowledge of microbe-metal interactions in environmental niches that impact atmospheric methane levels and are thus relevant to climate change.

scholarly journals Functional investigation of methanol dehydrogenase-like protein XoxF in Methylobacterium extorquens AM1

Microbiology ◽  
2010 ◽  
Vol 156 (8) ◽  
pp. 2575-2586 ◽  
Author(s):  
Sabrina Schmidt ◽  
Philipp Christen ◽  
Patrick Kiefer ◽  
Julia A. Vorholt
Keyword(s):  
Growth Parameters ◽  
Methanol Dehydrogenase ◽  
Plant Colonization ◽  
Kinetic Properties ◽  
Wild Type ◽  
Methylobacterium Extorquens ◽  
Experimental Conditions ◽  
Dependent Protein ◽  
One Carbon Metabolism ◽  
Functional Investigation

Methanol dehydrogenase-like protein XoxF of Methylobacterium extorquens AM1 exhibits a sequence identity of 50 % to the catalytic subunit MxaF of periplasmic methanol dehydrogenase in the same organism. The latter has been characterized in detail, identified as a pyrroloquinoline quinone (PQQ)-dependent protein, and shown to be essential for growth in the presence of methanol in this methylotrophic model bacterium. In contrast, the function of XoxF in M. extorquens AM1 has not yet been elucidated, and a phenotype remained to be described for a xoxF mutant. Here, we found that a xoxF mutant is less competitive than the wild-type during colonization of the phyllosphere of Arabidopsis thaliana, indicating a function for XoxF during plant colonization. A comparison of the growth parameters of the M. extorquens AM1 xoxF mutant with those of the wild-type during exponential growth revealed a reduced methanol uptake rate and a reduced growth rate for the xoxF mutant of about 30 %. Experiments with cells starved for carbon revealed that methanol oxidation in the xoxF mutant occurs less rapidly compared with the wild-type, especially in the first minutes after methanol addition. A distinct phenotype for the xoxF mutant was also observed when formate and CO2 production were measured after the addition of methanol or formaldehyde to starved cells. The wild-type, but not the xoxF mutant, accumulated formate upon substrate addition and had a 1 h lag in CO2 production under the experimental conditions. Determination of the kinetic properties of the purified enzyme showed a conversion capacity for both formaldehyde and methanol. The results suggest that XoxF is involved in one-carbon metabolism in M. extorquens AM1.

scholarly journals The Methanol Dehydrogenase Gene, mxaF, as a Functional and Phylogenetic Marker for Proteobacterial Methanotrophs in Natural Environments

PLoS ONE ◽  
2013 ◽  
Vol 8 (2) ◽  
pp. e56993 ◽  
Author(s):  
Evan Lau ◽  
Meredith C. Fisher ◽  
Paul A. Steudler ◽  
Colleen M. Cavanaugh
Keyword(s):  
Methanol Dehydrogenase ◽  
Natural Environments ◽  
Phylogenetic Marker ◽  
Dehydrogenase Gene
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