Novel metal sites in protein structures.
Recently, the three-dimensional structures of several novel metalloenzymes have been solved. Of special interest are those containing uncommon and/or not well characterized metals such as molybdenum, tungsten, nickel, vanadium and cobalt. Modulated by the protein environment, the specific properties of these metals and of special metal-binding cofactors such as siroheme and topa quinone are used to catalyze a vast array of fascinating reactions.
Volbeda
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Laboratoire de Cristallographie et de Cristallogénèse des Protéines, Institut de Biologie Structurale J P Ebel (CEA, CNRS), Grenoble, France. volbeda@lccp.ibs.fr
Fontecilla-Camps
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JC
Frey
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D001665:Binding Sites; D004798:Enzymes / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure
D004798:Enzymes; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D008670:Metals