Control of substrate access to the active site in methane monooxygenase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature11880.pdf
Reference37 articles.
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2. Merkx, M. et al. Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: A tale of two irons and three proteins. Angew. Chem. Int. Ed. Engl. 40, 2782–2807 (2001)
3. Wallar, B. J. & Lipscomb, J. D. Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96, 2625–2658 (1996)
4. Leahy, J. G., Batchelor, P. J. & Morcomb, S. M. Evolution of the soluble diiron monooxygenases. FEMS Microbiol. Rev. 27, 449–479 (2003)
5. Gassner, G. T. & Lippard, S. J. Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 38, 12768–12785 (1999)
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