ESR studies of protein A of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference25 articles.
1. Some properties of a soluble methane mono-oxygenase from Methylococcus capsulatus strain Bath
2. The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds
3. Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein
4. Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath).
5. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity.
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