Purification and characterisation of the soluble methane monooxygenase fromMethylosinus sporium5 demonstrates the highly conserved nature of this enzyme in methanotrophs-Reference-Cited by-同舟云学术

Purification and characterisation of the soluble methane monooxygenase fromMethylosinus sporium5 demonstrates the highly conserved nature of this enzyme in methanotrophs

Published:1991-02 Issue:1 Volume:78 Page:103-108
ISSN:0378-1097
Container-title:FEMS Microbiology Letters
language:en
Short-container-title:

Author:

Pilkington S.J.,Dalton H.

Publisher

Oxford University Press (OUP)

Subject

Genetics,Molecular Biology,Microbiology

Link

http://academic.oup.com/femsle/article-pdf/78/1/103/19091002/78-1-103.pdf

Reference14 articles.

1. Copper stress underlies the fundamental change in intracellular location of methane mono-oxygenase in methane-oxidizing organisms: Studies in batch and continuous cultures

2. Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath).

3. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity.

4. Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein

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1. Transcriptional regulation of soluble methane monooxygenase via enhancer-binding protein derived from Methylosinus sporium 5;Applied and Environmental Microbiology;2023-09-28

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3. Elucidation of the electron transfer environment in the MMOR FAD-binding domain from Methylosinus sporium 5;Dalton Transactions;2021

4. Compound-Specific Isotope Analysis for Studying the Biological Degradation of Hydrocarbons;Anaerobic Utilization of Hydrocarbons, Oils, and Lipids;2020

5. Biocatalytic Oxidations of Substrates through Soluble Methane Monooxygenase from Methylosinus sporium 5;Catalysts;2018-11-26