Localization of methanol dehydrogenase in two strains of methylotrophic bacteria detected by immunogold labeling

Fassel, Theresa A.; Buchholz, Lorie A.; Collins, Mary Lynne Perille; Remsen, Charles C.

doi:10.1128/aem.58.7.2302-2307.1992

Cited by 21 publications

(20 citation statements)

References 26 publications

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“…So far, existing experimental data on these parameters do not rule out any of these scenarios. The co-localization of pMMO and MeDH and reports of low O 2 /CH 4 ratios appear to support the hypothesis of direct coupling from methanol oxidation (Fassel et al, 1992;Kitmitto et al, 2005;Culpepper and Rosenzweig, 2014). Alternative systems present for formaldehyde and formate oxidation generate NAD(P)H, which could in turn be used to generate ubiquinol from ubiquinone (Trotsenko and Murrell, 2008;Vorholt 2002).…”

Section: Unsolved Problems In Methanotrophysupporting

confidence: 58%

“…In addition, heterologous expression of the wax ester synthase atfA may make it possible to produce fatty acid esters in some methanotrophic strains, as well as triacylglycerides if a diacylglycerol pool is present or generated (Janssen and Steinbuchel, 2014;Steen et al, 2010). Intriguingly, because methanol is generated from methane in methanotrophs, 513 it may be possible to produce fatty acid methyl esters (FAMEs) in situ without additional 514 modifications for alcohol synthesis (Fassel et al, 1992). It is therefore promising that some atfA homologs have significant activity with methanol for FAME production (Lee and Hu, 2010).…”

Section: Production Of Fatty Acid-derived Compounds From Methanotrophsmentioning

confidence: 99%

“…Anthony, 1982;Trotsenko and Khmelenina, 2008; Murrell, 2009, 2010; Winder, 238 2010;Jiang et al, 2010;Fei et al, 2014). However only a few methane-based products have 239 been made at the pilot-and commercial scales and so far, none of these have involved strains that 9 have been improved by metabolic engineering.…”

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confidence: 99%

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Metabolic engineering in methanotrophic bacteria

Kalyuzhnaya

Puri

Lidstrom

2015

Metabolic Engineering

277

162

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Methane, as natural gas or biogas, is the least expensive source of carbon for (bio)chemical synthesis. Scalable biological upgrading of this simple alkane to chemicals and fuels can bring new sustainable solutions to a number of industries with large environmental footprints, such as natural gas/petroleum production, landfills, wastewater treatment, and livestock. Microbial biocatalysis with methane as a feedstock has been pursued off and on for almost a half century, with little enduring success. Today, biological engineering and systems biology provide new opportunities for metabolic system modulation and give new optimism to the concept of a methane-based bio-industry. Here we present an overview of the most recent advances pertaining to metabolic engineering of microbial methane utilization. Some ideas concerning metabolic improvements for production of acetyl-CoA and pyruvate, two main precursors for bioconversion, are presented. We also discuss main gaps in the current knowledge of aerobic methane utilization, which must be solved in order to release the full potential of methane-based biosystems.

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Section: Unsolved Problems In Methanotrophysupporting

confidence: 58%

Section: Production Of Fatty Acid-derived Compounds From Methanotrophsmentioning

confidence: 99%

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Metabolic engineering in methanotrophic bacteria

Kalyuzhnaya

Puri

Lidstrom

2015

Metabolic Engineering

277

162

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“…In the methylotrophic bacterium Methylobacterium sp. AM 1 MDH was detected by immunogold labelling in the periplasmic space (FASSEL et al 1992). In fact it seems that MDH is loosely bound to the outer side of the cytoplasmic membrane and, depending on the membrane constitution and the method of cell breakage, respectively, it appears in different fractions.…”

Section: Discussionmentioning

confidence: 96%

Purification and properties of methanol dehydrogenase from Methylocystis sp. GB 25

Große

Wendlandt

Kleber

1997

J. Basic Microbiol.

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Methanol dehydrogenase (MDH) from Methylocystis sp. GB 25, which belongs to the group II of methanotrophic bacteria, is able to catalyse the oxidation of methanol to formate directly. The enzyme was purified 20-fold by a 5 step procedure to electrophoretic homogeneity. After cell disruption by French press, about 95% of MDH-activity was found in the soluble fraction. The relative molecular mass of the native enzyme has been estimated to be 122 kDa by gel filtration and 115 kDa by the method of Hedrick and Smith (1968). It seems to be composed of two identical subunits with a relative molecular mass of 62 kDa (estimated by SDS gel electrophoresis). The isoelectric point was found to be about 8.3. The amino terminal sequence shows a strong similarity to the alpha-chain of MDH from the facultative methylotrophic bacterium Methylobacterium extorquens AM1. PQQ, the probable prosthetic group of MDH, could be detected in the supernatant of the culture by using the apoenzyme of a membrane-bound glucose dehydrogenase from Pseudomonas aeruginosa but not absolutely in the absorption spectra of the enzyme after DEAE-chromatography. The purified MDH has an optimum activity at pH 9.0 and at 45 degrees C. MDH of Methylocystis sp. GB 25 oxidises only primary alcohols from methanol to heptanol and aldehydes from formaldehyde to propionaldehyde and the glutaraldehyde, respectively. The estimated Km-values show no dependence upon the chain length of substrates.

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“…First, MDH has been localized not only to the periplasm but also to the intracytoplasmic membranes in M. capsulatus (Bath) 17 as well as in the methanotrophs Methylomonas sp. strain A4 18 and Methylomicrobium album BG8. 19 Second, Dalton and co-workers reported the isolation, purification, and structural characterization of a complex containing both pMMO and MDH.…”

mentioning

confidence: 99%

Structure and Protein–Protein Interactions of Methanol Dehydrogenase from Methylococcus capsulatus (Bath)

Culpepper

Rosenzweig

2014

Biochemistry

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In the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Several lines of evidence suggest that the membrane-bound or particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex. To further investigate the possible existence of such a supercomplex, native MDH from Methylococcus capsulatus (Bath) has been purified and characterized by size exclusion chromatography with multi-angle light scattering and X-ray crystallography. M. capsulatus (Bath) MDH is primarily a dimer in solution, although an oligomeric species with a molecular mass of ∼450–560 kDa forms at higher protein concentrations. The 2.57 Å resolution crystal structure reveals an overall fold and α2β2 dimeric architecture similar to those of other MDH structures. In addition, biolayer interferometry studies demonstrate specific protein–protein interactions between MDH and M. capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of M. capsulatus (Bath) pMMO (spmoB). These interactions exhibit KD values of 833 ± 409 nM and 9.0 ± 7.7 μM, respectively. The biochemical data combined with analysis of the crystal lattice interactions observed in the MDH structure suggest a model in which MDH and pMMO associate not as a discrete, stoichiometric complex but as a larger assembly scaffolded by the intracytoplasmic membranes.

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Localization of methanol dehydrogenase in two strains of methylotrophic bacteria detected by immunogold labeling

Cited by 21 publications

References 26 publications

Metabolic engineering in methanotrophic bacteria

Metabolic engineering in methanotrophic bacteria

Purification and properties of methanol dehydrogenase from Methylocystis sp. GB 25

Structure and Protein–Protein Interactions of Methanol Dehydrogenase from Methylococcus capsulatus (Bath)

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