Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component.
TLDR
In this paper, the molybdenum cofactor has been isolated in an oxidized inactive form from purified molybinenzymes, and the isolated material is shown to be a novel pterin.About:
This article is published in Journal of Biological Chemistry.The article was published on 1980-03-10 and is currently open access. It has received 248 citations till now. The article focuses on the topics: Molybdenum cofactor & Pterin.read more
Citations
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Cell biology and molecular basis of denitrification.
TL;DR: Denitrification is intimately related to fundamental cellular processes that include primary and secondary transport, protein translocation, cytochrome c biogenesis, anaerobic gene regulation, metalloprotein assembly, and the biosynthesis of the cofactors molybdopterin and heme D1.
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The Mononuclear Molybdenum Enzymes
TL;DR: It is now well-established that all molybdenum-containing enzymes other than nitrogenase fall into three large and mutually exclusive families, as exemplified by the enzymes xanthine oxidation, sulfite oxidase, and DMSO reductase; these enzymes represent the focus of the present account.
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Nitrate respiration in relation to facultative metabolism in enterobacteria.
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Cell biology of molybdenum
Ralf R. Mendel,Florian Bittner +1 more
TL;DR: The transition element molybdenum (Mo) is of essential importance for (nearly) all biological systems as it is required by enzymes catalyzing diverse key reactions in the global carbon, sulfur and nitrogen metabolism.
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The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase.
TL;DR: The purification and initial characterization of arsenite oxidase from Alcaligenes faecalis are described, and a rhombic EPR signal appears which is similar to that of Rieske-type [2Fe-2S] clusters and spin quantifies to one spin/protein.
References
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Isolation of an iron-molybdenum cofactor from nitrogenase
Vinod K. Shah,Winston J. Brill +1 more
TL;DR: The FeMoCo might be used as a model for synthesizing catalysts for chemical nitrogen fixation and knowledge of the structure of this cofactor should be useful for understanding the role of molybdenum at the active site of nitrogenase, role of ligands close to moly bdenum in electron and proton transfer, and the catalytic mechanism of nitrogen fixation.
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A Common Co-Factor for Nitrate Reductase and Xanthine Dehydrogenase which also Regulates the Synthesis of Nitrate Reductase
TL;DR: A Common Co-Factor for Nitrate Reductase and Xanthine Dehydrogenase which also Regulates the Synthesis of NitrateReductase.
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A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on the subunit structure.
TL;DR: Pancreatinized enzyme has a greater mobility than unproteolyzed enzyme on polyacrylamide gels and is in good agreement with the minimum molecular weight of 157,000 calculated from dry weight determination and flavin analysis.
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In Vitro Formation of Assimilatory Reduced Nicotinamide Adenine Dinucleotide Phosphate: Nitrate Reductase from a Neurospora Mutant and a Component of Molybdenum-Enzymes
TL;DR: An active Neurospora-like assimilatory NADPH-nitrate reductase (EC 1.6.2) and several molybdenum-amino-acid complexes, as possible catalytic models of nitrogenase, were inactive (as were some previously tested 20 nonmolyb denum enzymes) in place of the acid-treated molyB denum-containing enzymes.
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