نتایج جستجو برای: methylosinus trichosporium

تعداد نتایج: 226  

Journal: :Applied and environmental microbiology 1990
D O Mountfort D White R A Asher

Cell suspensions of Methylosinus trichosporium oxidized the aromatic alcohols benzyl alcohol, vanillyl alcohol, and veratryl alcohol to the corresponding aldehydes, and with the exception of vanillyl alcohol, the aldehydes were further oxidized to the corresponding aromatic acids. No other transformation was observed, and the methoxyl moieties attached to the aromatic nucleus remained intact. M...

2001
Yi Liu Jay E. Dege

Kinetic, spectroscopic, and chemical evidence for the formation of specific catalytically essential complexes between the three protein components of the soluble form of methane monooxygenase from Methylosinus trichosporiurn OB3b is reported. The effects of the concentrations of the reductase and component B on the hydroxylation activity of the reconstituted enzyme system has been numerically s...

Journal: :Environmental microbiology 2013
Jeremy D Semrau Sheeja Jagadevan Alan A DiSpirito Ashraf Khalifa Julie Scanlan Brandt H Bergman Brittani C Freemeier Bipin S Baral Nathan L Bandow Alexey Vorobev Daniel H Haft Stéphane Vuilleumier J Colin Murrell

Biological oxidation of methane to methanol by aerobic bacteria is catalysed by two different enzymes, the cytoplasmic or soluble methane monooxygenase (sMMO) and the membrane-bound or particulate methane monooxygenase (pMMO). Expression of MMOs is controlled by a 'copper-switch', i.e. sMMO is only expressed at very low copper : biomass ratios, while pMMO expression increases as this ratio incr...

Journal: :Biotechnology progress 2000
E M Sipkema W de Koning K J Ganzeveld D B Janssen A A Beenackers

A biochemical model is presented that describes growth of Methylosinus trichosporium OB3b on methane. The model, which was developed to compare strategies to alleviate NADH limitation resulting from cometabolic contaminant conversion, includes (1) catabolism of methane via methanol, formaldehyde, and formate to carbon dioxide; (2) growth as formaldehyde assimilation; and (3) storage material (p...

Journal: :The Journal of biological chemistry 1994
C J Bender A C Rosenzweig S J Lippard J Peisach

Electron spin echo envelope modulation spectroscopy identified two ligand 14N interactions with the mixed-valence, Fe(II/III) diiron center of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath). Characteristic features of the spectra obtained at 9 and 10 GHz were analyzed and fit by simulation. One of the nitrogens possessed superhyperfine parameters (Aiso = 0.8 MHz, reff = ...

Journal: :The Biochemical journal 1973
A R Salem A J Hacking J R Quayle

1. Malyl-CoA lyase was found in high activity in extracts of Pseudomonas AM1, Pseudomonas MA, Pseudomonas MS, Hyphomicrobium X and Methylosinus trichosporium. 2. The enzyme cleaves (2S)-malyl-CoA into equimolar amounts of acetyl-CoA and glyoxylate in the presence of Mg(2+). 3. The specific activity of malyl-CoA lyase was several-fold higher in Pseudomonas AM1 when grown on C(1) compounds than w...

2005
JOHN COLBY DAVID I. STIRLING

1. Methane mono-oxygenase of Methylococcus capsulatus (Bath) catalyses the oxidation of various substituted methane derivatives including methanol. 2. It is a very non-specific oxygenase and, in some of its catalytic properties, apparently resembles the analogous enzyme from Methylomonas methanica but differs from those found in Methylosinus trichosporium and Methylomonas albus. 3. CO is oxidiz...

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