The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80690-I/fullpdf
Reference31 articles.
1. The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds
2. Degradation of trans-1,2-dichloroethene by mixed and pure cultures of methanotrophic bacteria
3. ESR studies of protein A of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
4. Structural characterization by EXAFS spectroscopy of the binuclear iron center in protein A of methane monooxygenase from Methylococcus capsulatus (Bath)
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