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XoxF-Type Methanol Dehydrogenase from the Anaerobic Methanotroph “Candidatus Methylomirabilis oxyfera” [PDF]
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Ming L Wu +2 more
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Functionality of the xoxF gene in Methylobacterium dichloromethanicum DM4
Microbiology, 2015Activation of expression of the xoxFgene encoding PQQ-dependent methanol/ethanol dehydrogenase (METDI2492) in dichloromethane- (DCM) -grown Methylobacterium dichloromethanicum DM4 was first demonstrated. The sequence of the only XoxF homolog found in the genome of strain DM4 exhibited 50% identity to that of the protein (MxaF) of the large subunit of ...
Yu E Firsova +2 more
exaly +3 more sources
Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C [PDF]
In methylotrophic bacteria, which use one-carbon (C1) compounds as a carbon source, methanol is oxidized by pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) enzymes. Methylotrophic genomes generally encode two distinct MDHs, MxaF and XoxF.
Yue Wen Deng +2 more
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XoxF Acts as the Predominant Methanol Dehydrogenase in the Type I Methanotroph Methylomicrobium buryatense [PDF]
ABSTRACT Many methylotrophic taxa harbor two distinct methanol dehydrogenase (MDH) systems for oxidizing methanol to formaldehyde: the well-studied calcium-dependent MxaFI type and the more recently discovered lanthanide-containing XoxF type.
Frances Chu, Mary E Lidström
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Antonie Van Leeuwenhoek, 2023
The impact of periplasmic localisation on the functioning of the XoxF protein was evaluated in the well-studied dichloromethane-utilising methylotroph Methylorubrum extorquens DM4, which harbors only one paralogue of the xoxF gene. It was found that the cytoplasmic targeting of XoxF by expression of the corresponding gene without the sequence encoding ...
Yulia E Firsova +2 more
exaly +3 more sources
The impact of periplasmic localisation on the functioning of the XoxF protein was evaluated in the well-studied dichloromethane-utilising methylotroph Methylorubrum extorquens DM4, which harbors only one paralogue of the xoxF gene. It was found that the cytoplasmic targeting of XoxF by expression of the corresponding gene without the sequence encoding ...
Yulia E Firsova +2 more
exaly +3 more sources
Investigation of XoxF methanol dehydrogenases reveals new methylotrophic bacteria in pelagic marine and freshwater ecosystems [PDF]
The diversity and distribution of methylotrophic bacteria have been investigated in the oceans and lakes using the methanol dehydrogenase mxaF gene as a functional marker. However, pelagic marine (OM43) and freshwater (LD28 and PRD01a001B) methylotrophs within the Betaproteobacteria lack mxaF, instead possessing a related xoxF4-encoded methanol ...
Arthi Ramachandran +2 more
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Characterization of a novel cytochrome c as the electron acceptor of XoxF-MDH in the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV [PDF]
Methanotrophs play a prominent role in the global carbon cycle, by oxidizing the potent greenhouse gas methane to CO2. Methane is first converted into methanol by methane monooxygenase. This methanol is subsequently oxidized by either a calcium-dependent MxaF-type or a lanthanide-dependent XoxF-type methanol dehydrogenase (MDH). Electrons from methanol
Wouter Versantvoort +2 more
exaly +3 more sources
Enzyme and Microbial Technology, 2020
XoxF-type methanol dehydrogenase was recently found to be lanthanide-dependent, while its counterpart MxaF is Ca2+-dependent. The lanthanide (Ln) series consists of 15 different elements, all of which exist in nature, although at different relative abundances.
Lun Wang +9 more
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XoxF-type methanol dehydrogenase was recently found to be lanthanide-dependent, while its counterpart MxaF is Ca2+-dependent. The lanthanide (Ln) series consists of 15 different elements, all of which exist in nature, although at different relative abundances.
Lun Wang +9 more
openaire +2 more sources
Chemistry – A European Journal, 2014
AbstractRare‐earth metal cations have recently been demonstrated to be essential co‐factors for the growth of the methanotrophic bacterium Methylacidiphilum fumariolicum SolV. A crystal structure of the rare‐earth‐dependent methanol dehydrogenase (MDH) includes a cerium cation in the active site. Herein, the Ce–MDH active site has been analyzed through
Justin A, Bogart +2 more
openaire +2 more sources
AbstractRare‐earth metal cations have recently been demonstrated to be essential co‐factors for the growth of the methanotrophic bacterium Methylacidiphilum fumariolicum SolV. A crystal structure of the rare‐earth‐dependent methanol dehydrogenase (MDH) includes a cerium cation in the active site. Herein, the Ce–MDH active site has been analyzed through
Justin A, Bogart +2 more
openaire +2 more sources

