scholarly journals Fractionation of the methane isotopologues 13CH4, 12CH3D, and 13CH3D during aerobic oxidation of methane by Methylococcus capsulatus (Bath)

2016 ◽  
Vol 192 ◽  
pp. 186-202 ◽  
Author(s):  
David T. Wang ◽  
Paula V. Welander ◽  
Shuhei Ono
Keyword(s):  
Aerobic Oxidation ◽  
Methylococcus Capsulatus ◽  
Oxidation Of Methane

scholarly journals Heterogeneously‐catalyzed aerobic oxidation of methane to a methyl derivative

2021 ◽  
Author(s):  
Jeroen A. van Bokhoven ◽  
Andrea N. Blankenship ◽  
Manoj Ravi ◽  
Mark A. Newton
Keyword(s):  
Aerobic Oxidation ◽  
Methyl Derivative ◽  
Oxidation Of Methane

Aerobic oxidation of methane to formaldehyde mediated by crystal-O over gold modified tungsten trioxide via photocatalysis

2021 ◽  
Vol 283 ◽  
pp. 119661
Author(s):  
Shilei Wei ◽  
Xianglian Zhu ◽  
Peiyun Zhang ◽  
Yingying Fan ◽  
Zhonghui Sun ◽  
...  
Keyword(s):  
Tungsten Trioxide ◽  
Aerobic Oxidation ◽  
Oxidation Of Methane

scholarly journals The metal centres of particulate methane mono-oxygenase

2008 ◽  
Vol 36 (6) ◽  
pp. 1134-1137 ◽  
Author(s):  
Amy C. Rosenzweig
Keyword(s):  
Crystal Structure ◽  
Reaction Mechanism ◽  
Structure Determination ◽  
Active Site ◽  
Spectroscopic Data ◽  
Present Review ◽  
Methylococcus Capsulatus ◽  
Research Groups ◽  
Oxidation Of Methane ◽  
Before And After

pMMO (particulate methane mono-oxygenase) is an integral membrane metalloenzyme that catalyses the oxidation of methane to methanol. The pMMO metal active site has not been identified, precluding detailed investigation of the reaction mechanism. Models for the metal centres proposed by various research groups have evolved as crystallographic and spectroscopic data have become available. The present review traces the evolution of these active-site models before and after the 2005 Methylococcus capsulatus (Bath) pMMO crystal structure determination.

Anaerobic and Aerobic Oxidation of Methane at Late Cretaceous Seeps in the Western Interior Seaway, USA

2006 ◽  
Vol 23 (7) ◽  
pp. 565-577 ◽  
Author(s):  
Daniel Birgel ◽  
Jörn Peckmann ◽  
Sandra Klautzsch ◽  
Volker Thiel ◽  
Joachim Reitner
Keyword(s):  
Late Cretaceous ◽  
Aerobic Oxidation ◽  
Western Interior Seaway ◽  
Oxidation Of Methane

scholarly journals A genome-scale metabolic model forMethylococcus capsulatuspredicts reduced efficiency uphill electron transfer to pMMO

2018 ◽  
Author(s):  
Christian Lieven ◽  
Leander A. H. Petersen ◽  
Sten Bay Jørgensen ◽  
Krist V. Gernaey ◽  
Markus J. Herrgard ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Metabolic Model ◽  
Single Cell Protein ◽  
Cell Protein ◽  
Methylococcus Capsulatus ◽  
Design Strategies ◽  
C1 Metabolism ◽  
Oxidation Of Methane ◽  
A Genome ◽  
Genome Scale

AbstractBackgroundGenome-scale metabolic models allow researchers to calculate yields, to predict consumption and production rates, and to study the effect of genetic modificationsin silico, without running resource-intensive experiments. While these models have become an invaluable tool for optimizing industrial production hosts likeE. coliandS. cerevisiae, few such models exist for one-carbon (C1) metabolizers.ResultsHere we present a genome-scale metabolic model forMethylococcus capsulatus, a well-studied obligate methanotroph, which has been used as a production strain of single cell protein (SCP). The model was manually curated, and spans a total of 877 metabolites connected via 898 reactions. The inclusion of 730 genes and comprehensive annotations, make this model not only a useful tool for modeling metabolic physiology, but also a centralized knowledge base forM. capsulatus. With it, we determined that oxidation of methane by the particulate methane monooxygenase is most likely driven through uphill electron transfer operating at reduced efficiency as this scenario matches best with experimental data from literature.ConclusionsThe metabolic model will serve the ongoing fundamental research of C1 metabolism, and pave the way for rational strain design strategies towards improved SCP production processes inM. capsulatus.

scholarly journals Steady-state kinetic analysis of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath)

1986 ◽  
Vol 236 (1) ◽  
pp. 155-162 ◽  
Author(s):  
J Green ◽  
H Dalton
Keyword(s):  
Steady State ◽  
Kinetic Analysis ◽  
Product Inhibition ◽  
Methylococcus Capsulatus ◽  
Reaction Sequence ◽  
Oxidation Of Methane ◽  
Steady State Kinetic ◽  
Substitution Mechanism ◽  
Inhibition Studies ◽  
State Kinetic

A steady-state kinetic analysis of purified soluble methane mono-oxygenase of Methylococcus capsulatus (Bath) was performed. The enzyme was found to follow a concerted-substitution mechanism. Methane binds to the enzyme followed by NADH, which reacts to yield reduced enzyme and NAD+. The reduced enzyme-methane complex binds O2 to give a second ternary complex, which breaks down to release water and methanol. In this way the enzyme can control the supply of electrons to the active site to coincide with the arrival of methane. Product-inhibition studies (with propylene as substrate) supported the reaction mechanism proposed. Ki values for NAD+ and propylene oxide are reported. The Km for NADH varied from 25 microM to 300 microM, depending on the nature of the hydrocarbon substrate, and thus supports the proposed reaction sequence. With methane as substrate the Km values for methane, NADH and O2 were shown to be 3 microM, 55.8 microM and 16.8 microM respectively. With propylene as substrate the Km values for propylene, NADH and O2 were 0.94 microM, 25.2 microM and 12.7-15.9 microM respectively. Methane mono-oxygenase was shown to be well adapted to the oxidation of methane compared with other straight-chain alkanes.

Aerobic Oxidation of Methane and Ethane by Unconventional Microbes at a Terrestrial Methane Seep in Sicily, Italy

2019 ◽  
Author(s):  
N. T. Smit ◽  
D. Rush ◽  
M. T. J. van der Meer ◽  
F. Grassa ◽  
L. Villlanueva ◽  
...  
Keyword(s):  
Aerobic Oxidation ◽  
Methane Seep ◽  
Oxidation Of Methane

Genes involved in the copper-dependent regulation of soluble methane monooxygenase of Methylococcus capsulatus (Bath): cloning, sequencing and mutational analysis

Microbiology ◽  
2003 ◽  
Vol 149 (7) ◽  
pp. 1785-1795 ◽  
Author(s):  
Róbert Csáki ◽  
Levente Bodrossy ◽  
József Klem ◽  
J. Colin Murrell ◽  
Kornél L. Kovács
Keyword(s):  
Fluorescent Protein ◽  
Mutational Analysis ◽  
Large Subunit ◽  
Methane Monooxygenase ◽  
Green Fluorescent Protein Gene ◽  
Methylococcus Capsulatus ◽  
Oxidation Of Methane ◽  
Soluble Methane Monooxygenase ◽  
Key Enzyme ◽  
Green Fluorescent

The key enzyme in methane metabolism is methane monooxygenase (MMO), which catalyses the oxidation of methane to methanol. Some methanotrophs, including Methylococcus capsulatus (Bath), possess two distinct MMOs. The level of copper in the environment regulates the biosynthesis of the MMO enzymes in these methanotrophs. Under low-copper conditions, soluble MMO (sMMO) is expressed and regulation takes place at the level of transcription. The structural genes of sMMO were previously identified as mmoXYBZ, mmoD and mmoC. Putative transcriptional start sites, containing a σ 70- and a σ N-dependent motif, were identified in the 5′ region of mmoX. The promoter region of mmoX was mapped using truncated 5′ end regions fused to a promoterless green fluorescent protein gene. A 9·5 kb region, adjacent to the sMMO structural gene cluster, was analysed. Downstream (3′) from the last gene of the operon, mmoC, four ORFs were found, mmoG, mmoQ, mmoS and mmoR. mmoG shows significant identity to the large subunit of the bacterial chaperonin gene, groEL. In the opposite orientation, two genes, mmoQ and mmoS, showed significant identity to two-component sensor–regulator system genes. Next to mmoS, a gene encoding a putative σ N-dependent transcriptional activator, mmoR was identified. The mmoG and mmoR genes were mutated by marker-exchange mutagenesis and the effects of these mutations on the expression of sMMO was investigated. sMMO transcription was impaired in both mutants. These results indicate that mmoG and mmoR are essential for the expression of sMMO in Mc. capsulatus (Bath).

scholarly journals Heterogeneously‐catalyzed aerobic oxidation of methane to a methyl derivative

2021 ◽  
Author(s):  
Jeroen A. van Bokhoven ◽  
Andrea N. Blankenship ◽  
Manoj Ravi ◽  
Mark A. Newton
Keyword(s):  
Aerobic Oxidation ◽  
Methyl Derivative ◽  
Oxidation Of Methane
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