Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism.
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.
Boll
Matthias
M
Institut für Biologie II, Universität Freiburg, Schänzlestr. 1, D-79104 Freiburg, Germany.
Schink
Bernhard
B
Messerschmidt
Albrecht
A
Kroneck
Peter M H
PM
D001421:Bacteria, Anaerobic / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008982:Molybdenum / Q000737:chemistry*; D011487:Protein Conformation; D013057:Spectrum Analysis; D014414:Tungsten / Q000737:chemistry*
D001426:Bacterial Proteins; D004798:Enzymes; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D008982:Molybdenum; D014414:Tungsten