J
Jean L. Johnson
Researcher at Duke University
Publications - 69
Citations - 4493
Jean L. Johnson is an academic researcher from Duke University. The author has contributed to research in topics: Sulfite oxidase & Molybdenum cofactor. The author has an hindex of 37, co-authored 69 publications receiving 4361 citations. Previous affiliations of Jean L. Johnson include National Institutes of Health.
Papers
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Journal ArticleDOI
The pterin molybdenum cofactors.
K.V. Rajagopalan,Jean L. Johnson +1 more
TL;DR: It is demonstrated that the inactive apoprotein of nitrate reductase in extracts of the mutant could be reconstituted by the addition of denatured preparations of purified molybdoenzymes from animal, fungal, or bacterial origin.
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Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component.
TL;DR: 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.
Journal ArticleDOI
Structural and metabolic relationship between the molybdenum cofactor and urothione.
Jean L. Johnson,K.V. Rajagopalan +1 more
TL;DR: The finding that urine samples from patients deficient in the molybdenum cofactor are devoid of urothione demonstrates a metabolic link between the two molecules, and a structural relationship is suggested.
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The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.
TL;DR: Results of chemical, mass spectral, and NMR studies are consistent with the side chain formulation -C identical to C--CH-OHCH2OPO2-3, indicating that molybdopterin is the phosphorylated analog of urothione but lacks the 3-methylthio function.
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Molecular Basis of the Biological Function of Molybdenum EFFECT OF TUNGSTEN ON XANTHINE OXIDASE AND SULFITE OXIDASE IN THE RAT
TL;DR: The results have been interpreted to indicate inhibition of molybdenum utilization by dietary tungsten, and the inability to effect such reactivation in vitro points to the requirement for activation or modification ofmolybdate as a prerequisite for prosthetic attachment to the enzymes.