Chemical Compound Review:
Molybdenum-101 molybdenum
Synonyms:
AC1L437P, 101Mo, 14191-83-4, Molybdenum, isotope of mass 101
- Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Boyington, J.C., Gladyshev, V.N., Khangulov, S.V., Stadtman, T.C., Sun, P.D. Science (1997)
- The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. Chan, M.K., Kim, J., Rees, D.C. Science (1993)
- Nickel and molybdenum contact allergies in patients with coronary in-stent restenosis. Köster, R., Vieluf, D., Kiehn, M., Sommerauer, M., Kähler, J., Baldus, S., Meinertz, T., Hamm, C.W. Lancet (2000)
- Metal and sulfur composition of iron-molybdenum cofactor of nitrogenase. Nelson, M.J., Levy, M.A., Orme-Johnson, W.H. Proc. Natl. Acad. Sci. U.S.A. (1983)
- Zn, Cu and Co in cyanobacteria: selective control of metal availability. Cavet, J.S., Borrelly, G.P., Robinson, N.J. FEMS Microbiol. Rev. (2003)
- Formation of thermally stable alkylidene layers on a catalytically active surface. Zahidi, E.M., Oudghiri-Hassani, H., McBreen, P.H. Nature (2001)
- Localization of a gene for molybdenum cofactor deficiency, on the short arm of chromosome 6, by homozygosity mapping. Shalata, A., Mandel, H., Reiss, J., Szargel, R., Cohen-Akenine, A., Dorche, C., Zabot, M.T., Van Gennip, A., Abeling, N., Berant, M., Cohen, N. Am. J. Hum. Genet. (1998)
- Molybdenum cofactor deficiency-phenotypic variability in a family with a late-onset variant. Hughes, E.F., Fairbanks, L., Simmonds, H.A., Robinson, R.O. Developmental medicine and child neurology. (1998)
- Molybdenum trioxide nanostructures: the evolution from helical nanosheets to crosslike nanoflowers to nanobelts. Li, G., Jiang, L., Pang, S., Peng, H., Zhang, Z. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical (2006)
- Molybdenum-cofactor-containing enzymes: structure and mechanism. Kisker, C., Schindelin, H., Rees, D.C. Annu. Rev. Biochem. (1997)
- Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Kisker, C., Schindelin, H., Pacheco, A., Wehbi, W.A., Garrett, R.M., Rajagopalan, K.V., Enemark, J.H., Rees, D.C. Cell (1997)
- Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity. Feng, G., Tintrup, H., Kirsch, J., Nichol, M.C., Kuhse, J., Betz, H., Sanes, J.R. Science (1998)
- Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Georgiadis, M.M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J.J., Rees, D.C. Science (1992)
- Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. Ichida, K., Amaya, Y., Kamatani, N., Nishino, T., Hosoya, T., Sakai, O. J. Clin. Invest. (1997)
- The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds. Hall, D.R., Gourley, D.G., Leonard, G.A., Duke, E.M., Anderson, L.A., Boxer, D.H., Hunter, W.N. EMBO J. (1999)
- Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme. Gladyshev, V.N., Khangulov, S.V., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (1994)
- Isolation of a molybdenum--iron cluster from nitrogenase. Shah, V.K., Brill, W.J. Proc. Natl. Acad. Sci. U.S.A. (1981)
- Effect of dietary molybdenum on esophageal carcinogenesis in rats induced by N-methyl-N-benzylnitrosamine. Komada, H., Kise, Y., Nakagawa, M., Yamamura, M., Hioki, K., Yamamoto, M. Cancer Res. (1990)
- The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters. Rothery, R.A., Magalon, A., Giordano, G., Guigliarelli, B., Blasco, F., Weiner, J.H. J. Biol. Chem. (1998)
- Nitrogenases without molybdenum. Pau, R.N. Trends Biochem. Sci. (1989)
- Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Su, W., Huber, S.C., Crawford, N.M. Plant Cell (1996)
- Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. Arnoux, P., Sabaty, M., Alric, J., Frangioni, B., Guigliarelli, B., Adriano, J.M., Pignol, D. Nat. Struct. Biol. (2003)
- The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition. Okamoto, K., Matsumoto, K., Hille, R., Eger, B.T., Pai, E.F., Nishino, T. Proc. Natl. Acad. Sci. U.S.A. (2004)
- Diversity and phylogeny of gephyrin: tissue-specific splice variants, gene structure, and sequence similarities to molybdenum cofactor-synthesizing and cytoskeleton-associated proteins. Ramming, M., Kins, S., Werner, N., Hermann, A., Betz, H., Kirsch, J. Proc. Natl. Acad. Sci. U.S.A. (2000)
- A mutation in the gene for the neurotransmitter receptor-clustering protein gephyrin causes a novel form of molybdenum cofactor deficiency. Reiss, J., Gross-Hardt, S., Christensen, E., Schmidt, P., Mendel, R.R., Schwarz, G. Am. J. Hum. Genet. (2001)
- The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells. Stallmeyer, B., Schwarz, G., Schulze, J., Nerlich, A., Reiss, J., Kirsch, J., Mendel, R.R. Proc. Natl. Acad. Sci. U.S.A. (1999)
- Identification of the Missing Component in the Mitochondrial Benzamidoxime Prodrug-converting System as a Novel Molybdenum Enzyme. Havemeyer, A., Bittner, F., Wollers, S., Mendel, R., Kunze, T., Clement, B. J. Biol. Chem. (2006)
- Molybdenum content of human milk. Casey, C.E. Am. J. Clin. Nutr. (1989)
- Human sulfite oxidase deficiency. Characterization of the molecular defect in a multicomponent system. Johnson, J.L., Rajagopalan, K.V. J. Clin. Invest. (1976)
- Structural and Electron Paramagnetic Resonance (EPR) Studies of Mononuclear Molybdenum Enzymes from Sulfate-Reducing Bacteria. Brondino, C.D., Rivas, M.G., Rom??o, M.J., Moura, J.J., Moura, I. Acc. Chem. Res. (2006)
- Second gene (nifH*) coding for a nitrogenase iron protein in Azotobacter chroococcum is adjacent to a gene coding for a ferredoxin-like protein. Robson, R., Woodley, P., Jones, R. EMBO J. (1986)
- Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site. Fischer, K., Barbier, G.G., Hecht, H.J., Mendel, R.R., Campbell, W.H., Schwarz, G. Plant Cell (2005)
- Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases. Reyes, F., Roldán, M.D., Klipp, W., Castillo, F., Moreno-Vivián, C. Mol. Microbiol. (1996)
- Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase. Leimkühler, S., Charcosset, M., Latour, P., Dorche, C., Kleppe, S., Scaglia, F., Szymczak, I., Schupp, P., Hahnewald, R., Reiss, J. Hum. Genet. (2005)
- The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain. Rudolph, M.J., Johnson, J.L., Rajagopalan, K.V., Kisker, C. Acta Crystallogr. D Biol. Crystallogr. (2003)
- Activation in vitro of respiratory nitrate reductase of Escherichia coli K12 grown in the presence of tungstate. Involvement of molybdenum cofactor. Saracino, L., Violet, M., Boxer, D.H., Giordano, G. Eur. J. Biochem. (1986)
- Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Rudolph, M.J., Wuebbens, M.M., Rajagopalan, K.V., Schindelin, H. Nat. Struct. Biol. (2001)
- Consequences of removal of a molybdenum ligand (DmsA-Ser-176) of Escherichia coli dimethyl sulfoxide reductase. Trieber, C.A., Rothery, R.A., Weiner, J.H. J. Biol. Chem. (1996)
- Resonance-enhanced Raman scattering from the molybdenum center of xanthine oxidase. Oertling, W.A., Hille, R. J. Biol. Chem. (1990)