[ASAP] Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues
[ASAP] Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues
Mechanism of Flavoprotein l-6-HydroxynicotineOxidase: pH and Solvent Isotope Effects and Identification of KeyActive Site Residues
Mechanism of Flavoprotein l-6-HydroxynicotineOxidase: pH and Solvent Isotope Effects and Identification of KeyActive Site Residues
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01160/20170126/images/medium/bi-2016-01160d_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01160
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Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01325/20160115/images/medium/bi-2015-01325p_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01325
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01-16-2016 04:41 AM
Active site dynamics in NADH oxidase from Thermus thermophilus studied by NMR spin relaxation
Active site dynamics in NADH oxidase from Thermus thermophilus studied by NMR spin relaxation
Abstract We have characterized the backbone dynamics of NADH oxidase from Thermus thermophilus (NOX) using a recently-developed suite of NMR experiments designed to isolate exchange broadening, together with 15N R 1, R 1Ï? , and {1H}-15N steady-state NOE relaxation measurements performed at 11.7 and 18.8 T. NOX is a 54 kDa homodimeric enzyme that belongs to a family of structurally homologous flavin reductases and nitroreductases with many potential biotechnology applications. Prior studies...
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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08-30-2011 04:52 PM
[NMR paper] The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic
The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
Related Articles The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
Biochemistry. 2004 Apr 13;43(14):4082-91
Authors: Azurmendi HF, Wang SC, Massiah MA, Poelarends GJ, Whitman CP, Mildvan AS
trans-3-Chloroacrylic acid dehalogenase (CaaD) converts trans-3-chloroacrylic acid to malonate semialdehyde by the...
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11-24-2010 09:51 PM
[NMR paper] NMR observation of substrate in the binding site of an active sugar-H+ symport protei
NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.
Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3877-81
Authors: Spooner PJ, Rutherford NG, Watts A, Henderson PJ
NMR methods have been adopted to observe directly the characteristics of substrate...
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08-22-2010 03:33 AM
[NMR paper] Involvement of various amino- and carboxyl-terminal residues in the active site of th
Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins.
Related Articles Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with...
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[ASAP] Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues
Linear Mode
