(Q46338208)

English

The particulate methane monooxygenase from methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization

scientific article published in April 1998

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scholarly article

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

The particulate methane monooxygenase from methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization (English)

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

1 reference

based on heuristic

inferred from title

Methylococcus capsulatus

object named as

methylococcus capsulatus

1 reference

based on heuristic

inferred from title

Sean J. Elliott

2

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

author name string

Nguyen HH

1

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

Yip JH

3

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

Chan SI

4

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

language of work or name

0 references

publication date

1 April 1998

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

Journal of Biological Chemistry

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

273

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

14

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

7957-7966

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

Biochemistry of the soluble methane monooxygenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

The role of copper in the pMMO of Methylococcus capsulatus bath: a structural vs. catalytic function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Purification and Properties of a Soluble Methane Monooxygenase from Methylocystis sp. M.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Particulate methane monooxygenase genes in methanotrophs

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

The purification of ammonia monooxygenase from Paracoccus denitrificans.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Sequence of an ammonia monooxygenase subunit A-encoding gene from Nitrosospira sp. NpAV.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Comparative analysis of gene sequences encoding ammonia monooxygenase of Nitrosospira sp. AHB1 and Nitrosolobus multiformis C-71.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

The gene encoding ammonia monooxygenase subunit A exists in three nearly identical copies in Nitrosospira sp. NpAV.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Spectroscopic properties of the hydroxylase of methane monooxygenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Gating Effects of Component B on Oxygen Activation by the Methane Monooxygenase Hydroxylase Component

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.14.7957

21 January 2018

Identifiers

10.1074/JBC.273.14.7957

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/9525893

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