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Dimitri Niks

Showing results (1-10 of 57) with videos related to

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Methods in Enzymology|April 25, 2022
Application of EPR and related methods to molybdenum-containing enzymesRuss Hille, Dimitri Niks
Methods in Molecular Biology (Clifton, N.J.)|October 15, 2018
Molybdenum-Containing EnzymesDimitri Niks, Russ Hille
Methods in Enzymology|December 5, 2018
Reductive activation of CO<sub>2</sub> by formate dehydrogenasesDimitri Niks, Russ Hille
Protein Science : a Publication of the Protein Society|August 19, 2018
Molybdenum- and tungsten-containing formate dehydrogenases and formylmethanofuran dehydrogenases: Structure, mechanism, and cofactor insertionDimitri Niks, Russ Hille
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|January 5, 2018
Kinetic and spectroscopic characterization of tungsten-substituted DMSO reductase from Rhodobacter sphaeroidesJosué Pacheco, Dimitri Niks, Russ Hille
Journal of Inorganic Biochemistry|March 21, 2022
The air-inactivation of formate dehydrogenase FdsDABG from Cupriavidus necatorSheron Hakopian, Dimitri Niks, Russ Hille
The Journal of Biological Chemistry|September 5, 2024
The rapid-reaction kinetics of an electron-bifurcating flavoprotein, the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase EtfAB:bcdDerek Nguyen, Wayne Vigil, Dimitri Niks, et al.
The Journal of Biological Chemistry|November 11, 2015
Spectroscopic and Kinetic Properties of the Molybdenum-containing, NAD+-dependent Formate Dehydrogenase from Ralstonia eutrophaDimitri Niks, Jayant Duvvuru, Miguel Escalona, et al.
The Journal of Biological Chemistry|August 9, 2017
Efficient reduction of CO<sub>2</sub> by the molybdenum-containing formate dehydrogenase from <i>Cupriavidus necator</i> (<i>Ralstonia eutropha</i>)Xuejun Yu, Dimitri Niks, Ashok Mulchandani, et al.
Acta Crystallographica. Section D, Biological Crystallography|July 4, 2012
The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding propertyEduardo Hilario, Yang Li, Dimitri Niks, et al.
Pageof 6

Showing results (1-10 of 57) with videos related to

Sort By:
Pageof 6
Methods in Enzymology|April 25, 2022
Application of EPR and related methods to molybdenum-containing enzymesRuss Hille, Dimitri Niks
Methods in Molecular Biology (Clifton, N.J.)|October 15, 2018
Molybdenum-Containing EnzymesDimitri Niks, Russ Hille
Methods in Enzymology|December 5, 2018
Reductive activation of CO<sub>2</sub> by formate dehydrogenasesDimitri Niks, Russ Hille
Protein Science : a Publication of the Protein Society|August 19, 2018
Molybdenum- and tungsten-containing formate dehydrogenases and formylmethanofuran dehydrogenases: Structure, mechanism, and cofactor insertionDimitri Niks, Russ Hille
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|January 5, 2018
Kinetic and spectroscopic characterization of tungsten-substituted DMSO reductase from Rhodobacter sphaeroidesJosué Pacheco, Dimitri Niks, Russ Hille
Journal of Inorganic Biochemistry|March 21, 2022
The air-inactivation of formate dehydrogenase FdsDABG from Cupriavidus necatorSheron Hakopian, Dimitri Niks, Russ Hille
The Journal of Biological Chemistry|September 5, 2024
The rapid-reaction kinetics of an electron-bifurcating flavoprotein, the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase EtfAB:bcdDerek Nguyen, Wayne Vigil, Dimitri Niks, et al.
The Journal of Biological Chemistry|November 11, 2015
Spectroscopic and Kinetic Properties of the Molybdenum-containing, NAD+-dependent Formate Dehydrogenase from Ralstonia eutrophaDimitri Niks, Jayant Duvvuru, Miguel Escalona, et al.
The Journal of Biological Chemistry|August 9, 2017
Efficient reduction of CO<sub>2</sub> by the molybdenum-containing formate dehydrogenase from <i>Cupriavidus necator</i> (<i>Ralstonia eutropha</i>)Xuejun Yu, Dimitri Niks, Ashok Mulchandani, et al.
Acta Crystallographica. Section D, Biological Crystallography|July 4, 2012
The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding propertyEduardo Hilario, Yang Li, Dimitri Niks, et al.
Pageof 6