Browsing by Subject "Molybdenum"

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    A Comparison of the Ligation Torque Expression of a Ribbonwise Bracket–Archwire Combination and a Conventional Combination: A Primary Study
    (Hindawi, 2022-09-28) Lin, Bin; Jiang, Feifei; Chen, Jie; Liang, Jiaxing; Mechanical and Energy Engineering, Purdue School of Engineering and Technology
    Objective: To assess the effect of the third-order mechanics of a new ribbonwise bracket-archwire combination using an orthodontic torque simulator. Material and Methods. An orthodontic torque simulator was used to measure the third-order moment of a maxillary central incisor as it changed from a neutral position to a 40° rotation in 1° increment. A new ribbonwise bracket (Xinya, China) was compared with a conventional ligation bracket (American Orthodontic, U.S.A.). The effects of different archwire sizes (i.e., 0.017″ × 0.025″ and 0.019″ × 0.025″) and materials (i.e., nickel-titanium, titanium-molybdenum alloy, and stainless steel) were analyzed. Paired sample t-tests were conducted to compare the moments between the two bracket types corresponding to each of the archwires. The effects of the stiffness of the bracket-archwire complexes were also assessed. Results: Statistically significant differences (P=0.05) between the moments from the two brackets were found. The ribbonwise bracket-archwire complex generated larger moments when the rotation angle was lower than 30°. The ribbonwise brackets produced moments that could reach a threshold of 5 Nmm more quickly as the angle was increased. The higher the stiffness of the complex, the larger the moment. Conclusion: The ribbonwise bracket-archwire complex reached the moment threshold limits earlier than the conventional complex. When the rotation angle is less than 30°, the ribbonwise bracket-archwire complex generated a greater torque moment in comparison with the conventional complex.
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    Molecular cloning, expression and biochemical characterization of periplasmic nitrate reductase from Campylobacter jejuni
    (Oxford University Press, 2018-08-01) Mintmier, Breeanna; McGarry, Jennifer M.; Sparacino-Watkins, Courtney E.; Sallmen, Joseph; Fischer-Schrader, Katrin; Magalon, Axel; McCormick, Joseph R.; Stolz, John F.; Schwarz, Günter; Bain, Daniel J.; Basu, Partha; Chemistry and Chemical Biology, School of Science
    Campylobacter jejuni, a human gastrointestinal pathogen, uses nitrate for growth under microaerophilic conditions using periplasmic nitrate reductase (Nap). The catalytic subunit, NapA, contains two prosthetic groups, an iron sulfur cluster and a molybdenum cofactor. Here we describe the cloning, expression, purification, and Michaelis-Menten kinetics (kcat of 5.91 ± 0.18 s-1 and a KM (nitrate) of 3.40 ± 0.44 μM) in solution using methyl viologen as an electron donor. The data suggest that the high affinity of NapA for nitrate could support growth of C. jejuni on nitrate in the gastrointestinal tract. Site-directed mutagenesis was used and the codon for the molybdenum coordinating cysteine residue has been exchanged for serine. The resulting variant NapA is 4-fold less active than the native enzyme confirming the importance of this residue. The properties of the C. jejuni enzyme reported here represent the first isolation and characterization of an epsilonproteobacterial NapA. Therefore, the fundamental knowledge of Nap has been expanded.