Novel bacterial molybdenum and tungsten enzymes : three-dimensional structure, spectroscopy, and reaction mechanism

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2005
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Boll, Matthias
Messerschmidt, A.
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Biological Chemistry. 2005, 386(10), pp. 999-2006
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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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570 Biowissenschaften, Biologie
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ISO 690BOLL, 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. 2005, 386(10), pp. 999-2006
BibTex
@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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