Redox Potentiometry Studies of Particulate Methane Monooxygenase: Support for a Trinuclear Copper Cluster Active Site
Authors:
- 2 March 2007
- journal article
- zuschrift
- Published by Wiley in Angewandte Chemie
- Vol. 119 (12) , 2038-2040
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methaneNature, 2005
- The quest for the particulate methane monooxygenase active siteDalton Transactions, 2005
- Study on the Solid Phase Extraction of Hg(II)‐ABR Chelate with C18 Disks and its Application to the Determination of Mercury in Tobacco and Tobacco AdditivesJournal of the Chinese Chemical Society, 2004
- Biological Methane Oxidation: Regulation, Biochemistry, and Active Site Structure of Particulate Methane MonooxygenaseCritical Reviews in Biochemistry and Molecular Biology, 2004
- Production of High-Quality Particulate Methane Monooxygenase in High Yields from Methylococcus capsulatus (Bath) with a Hollow-Fiber Membrane BioreactorJournal of Bacteriology, 2003
- The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus BathJournal of Bacteriology, 2003
- Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing clusterProceedings of the National Academy of Sciences, 2003
- The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron proteinBiochemical Journal, 2003
- The Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath) Is a Novel Copper-containing Three-subunit EnzymeJournal of Biological Chemistry, 1998
- X-ray Absorption and EPR Studies on the Copper Ions Associated with the Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath). Cu(I) Ions and Their ImplicationsJournal of the American Chemical Society, 1996