Novel bacterial molybdenum and tungsten enzymes : three-dimensional structure, spectroscopy, and reaction mechanism
Novel bacterial molybdenum and tungsten enzymes : three-dimensional structure, spectroscopy, and reaction mechanism
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2005
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Biological Chemistry ; 386 (2005), 10. - pp. 999-2006
Abstract
The molybdenum enzymes 4-hydroxybenzoyl-CoA reductase and pyrogallol-phloroglucinol transhydroxylase and the tungsten enzyme acetylene hydratase catalyze reductive dehydroxylation reactions, i.e., transhydroxylation between phenolic residues and the addition of water to a triple bond. Such activities are unusual for this class of enzymes, which carry either a mononuclear Mo or W center. Crystallization and subsequent structural analysis by high-resolution X-ray crystallography has helped to resolve the reaction centers of these enzymes to a degree that allows us to understand the interaction of the enzyme and the respective substrate(s) in detail, and to develop a concept for the respective reaction mechanism, at least in two cases.
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BOLL, Matthias, Bernhard SCHINK, A. MESSERSCHMIDT, Peter M. H. KRONECK, 2005. Novel bacterial molybdenum and tungsten enzymes : three-dimensional structure, spectroscopy, and reaction mechanism. In: Biological Chemistry. 386(10), pp. 999-2006BibTex
@article{Boll2005Novel-7162, year={2005}, title={Novel bacterial molybdenum and tungsten enzymes : three-dimensional structure, spectroscopy, and reaction mechanism}, number={10}, volume={386}, journal={Biological Chemistry}, pages={999--2006}, author={Boll, Matthias and Schink, Bernhard and Messerschmidt, A. and Kroneck, Peter M. H.} }
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