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Catlin DS, Yang X, Bennett B, et al. (2020) Structural basis for the hydrolytic dehalogenation of the fungicide chlorothalonil. The Journal of Biological Chemistry |
Nocek B, Reidl C, Starus A, et al. (2017) Structural Evidence for a Major Conformational Change Triggered by Substrate Binding in DapE Enzymes: Impact on the Catalytic Mechanism. Biochemistry |
Stein N, Gumataotao N, Hajnas N, et al. (2017) Multiple States of Nitrile Hydratase from Rhodococcus equi TG328-2: Structural and Mechanistic Insights from EPR and DFT Studies. Biochemistry |
Martinez S, Wu R, Krzywda K, et al. (2015) Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 20: 885-94 |
Martinez S, Wu R, Sanishvili R, et al. (2014) The active site sulfenic acid ligand in nitrile hydratases can function as a nucleophile. Journal of the American Chemical Society. 136: 1186-9 |
McGregor WC, Gillner DM, Swierczek SI, et al. (2013) Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli. Springerplus. 2: 482 |
Gumataotao N, Kuhn ML, Hajnas N, et al. (2013) Identification of an active site-bound nitrile hydratase intermediate through single turnover stopped-flow spectroscopy. The Journal of Biological Chemistry. 288: 15532-6 |
Gillner DM, Becker DP, Holz RC. (2013) Lysine biosynthesis in bacteria: a metallodesuccinylase as a potential antimicrobial target. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 18: 155-63 |
Kuhn ML, Martinez S, Gumataotao N, et al. (2012) The Fe-type nitrile hydratase from Comamonas testosteroni Ni1 does not require an activator accessory protein for expression in Escherichia coli. Biochemical and Biophysical Research Communications. 424: 365-70 |
Tao Y, Shokes JE, McGregor WC, et al. (2012) Structural characterization of Zn(II)-, Co(II)-, and Mn(II)-loaded forms of the argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli. Journal of Inorganic Biochemistry. 111: 157-63 |