Results 21 to 30 of about 945 (112)
Synthesis, characterization, and spectroscopy of model molybdopterin complexes [PDF]
Journal of Inorganic Biochemistry, 2007 The preparation and characterization of new model complexes for the molybdenum cofactor are reported. The new models are distinctive for the inclusion of pterin-substituted dithiolene chelates and have the formulation Tp(*)MoX(pterin-R-dithiolene) (Tp(*)=tris(3,5,-dimethylpyrazolyl)borate), X=O, S, R=aryl.
Sharon J Nieter, Burgmayer +10 more
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A regioselective synthesis of the dephospho ditholene protected molybdopterin [PDF]
RSC Adv., 2014 Regioselective condensation.
Igor V, Pimkov +3 more
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Genetic Evidence for a Molybdopterin-Containing Tellurate Reductase [PDF]
Applied and Environmental Microbiology, 2013 ABSTRACT The genetic identity and cofactor composition of the bacterial tellurate reductase are currently unknown. In this study, we examined the requirement of molybdopterin biosynthesis and molybdate transporter genes for tellurate reduction in Escherichia coli K-12. The results show that mutants deleted
Joanne, Theisen +2 more
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Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria [PDF]
Journal of Bacteriology, 1984 The carbon monoxide oxidases (COXs) purified from the carboxydotrophic bacteria Pseudomonas carboxydohydrogena and Pseudomonas carboxydoflava were found to be molybdenum hydroxylases, identical in cofactor composition and spectral properties to the recently characterized enzyme from Pseudomonas carboxydovorans (O. Meyer, J. Biol. Chem.
O, Meyer, K V, Rajagopalan
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In Vitro Molybdenum Ligation to Molybdopterin Using Purified Components [PDF]
Journal of Biological Chemistry, 2005 We have previously shown that Escherichia coli MoeA and MogA are required in vivo for the final step of molybdenum cofactor biosynthesis, the addition of the molybdenum atom to the dithiolene of molybdopterin. MoeA was also shown to facilitate the addition of molybdenum in an assay using crude extracts from E. coli moeA(-) cells.
Jason D, Nichols, K V, Rajagopalan
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An IscS Persulfide Donates the Sulfur for Ribosomal Protein uL16 Thioamidation
Angewandte Chemie International Edition, EarlyView.YcaO‐catalyzed thioamidation of the ribosomal subunit protein uL16 is widespread in Pseudomonadota bacteria. We identify the iron–sulfur cluster cysteine desulfurase IscS as the sulfur donor via an IscS persulfide and observe direct IscS–uL16 interactions.
Yanqing Xue +2 more
wiley +1 more source
Occurrence of Nitrate Reductase and Molybdopterin in Xanthomonas maltophilia [PDF]
Applied and Environmental Microbiology, 1990 Fifteen of 23 ATCC strains and 2 of 9 clinical isolates of Xanthomonas maltophilia , all of which grew aerobically on ammonia, but not nitrate, as a sole nitrogen source, reduced nitrate to nitrite. X. maltophilia failed to grow anaerobically on complex medium with or without nitrate, so it ...
L M, Woodard +3 more
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Enzymatic Electrosynthesis for Sustainable CO2 Conversion: Advancing Circular Carbon Economy
Carbon Energy, EarlyView.Enzymatic electrosynthesis (EES) offers molecular precision in synthesizing value‐added products from CO2. We highlight its distinct edge over alternative enzyme‐hybrid systems and analyze electron transfer pathways. Key strategies to overcome electron transfer bottlenecks and expand product diversity are addressed, and also data‐driven approaches for ...
Yan Xie +7 more
wiley +1 more source
Molybdopterin cofactor from Methanobacterium formicicum formate dehydrogenase [PDF]
Journal of Bacteriology, 1986 The molybdopterin cofactor from the formate dehydrogenase of Methanobacterium formicicum was studied. The cofactor was released by guanidine denaturation of homogeneous enzyme, which also released greater than 80% of the molybdenum present in the enzyme.
H D, May, N L, Schauer, J G, Ferry
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One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives
ChemBioChem, Volume 27, Issue 19, 14 October 2026.The terminal sulfido ligand in mononuclear molybdoenzymes has been appreciated for almost 125 years, with the characterization of Schardinger's enzyme in cow's milk, now known to be xanthine oxidase, that was isolated in 1902 in Vienna, Austria. The ligand is found in molybdoenzymes identified across all kingdoms of life.
Silke Leimkühler +2 more
wiley +1 more source