New Pyranopterin Chemistry Related to Molybdenum and Tungsten Enzymes
A large group of molybdo- and tungstoenzymes utilizes “molybdopterin,” a hydrogenated pterin component, in the molybdenum cofactor (Moco) (1). Recent X-ray crystal structures of metal-molybdopterin enzymes have revealed at least three different structural types for Moco (2). Common to all of the crystal structures, however, is the coordination of the metal center by sulfur donors from the dithiolene groups of one or two molybdopterins. Additionally, the data show that the pterin portion is present in a previously unreported tricyclic form including a pyrano ring.
Unable to display preview. Download preview PDF.
- 1.R. S. Pilato and E. I. Stiefel in Bioinorganic Catalysis (J. Reedijk, E. Bouwman eds.), Marcel Dekker, New York, pp. 81–152, 1999.Google Scholar
- 2.C. Kisker, H. Schindelin and D. C. Rees, Annu. Rev. Biochem., 66: 233–267, 1997; C. Kisker, H. Schindelin, D. Baas, J. Rétey, R. U. Meckenstock and P. M. H. Kroneck, FEMS Microbiol. Rev., 22: 503–521 (1999); R. Hille, J. Rétey, U. Bartlewski-Hof, W. Reichenbecher and B. Schink, FEMS Microbiol. Rev., 22: 489–501, 1999.PubMedCrossRefGoogle Scholar
- 3.B. Fischer, M. vom Orde, K. Leidenberger, A. Pacheco and L. Bigler in Chem. Biol. Pteridines, Proc. 11th Int. Symp. Pteridines and Folates (W. Pfleiderer, H. Rokos, eds.) Blackwell Science, Berlin, Vienna, Fed. Rep. Ger., pp. 23–28, 1997.Google Scholar
- 5.J. N. Low, E. Cadoret, G. Ferguson, M.D. Lopez, M.L. Quijano, A. Sanchez and M. Nogueras Acta Cryst, C51: 2141–2143, 1995.Google Scholar
- 6.B. Bradshaw, D. Collison, C. D. Garner, J. A. Joule, Chem. Commun., 123–124, 2001.Google Scholar