Year |
Citation |
Score |
2013 |
Casey TM, Grzyska PK, Hausinger RP, McCracken J. Measuring the orientation of taurine in the active site of the non-heme Fe(II)/α-ketoglutarate-dependent taurine hydroxylase (TauD) using electron spin echo envelope modulation (ESEEM) spectroscopy. The Journal of Physical Chemistry. B. 117: 10384-94. PMID 23937570 DOI: 10.1021/Jp404743D |
0.305 |
|
2010 |
Grzyska PK, Appelman EH, Hausinger RP, Proshlyakov DA. Insight into the mechanism of an iron dioxygenase by resolution of steps following the FeIV=HO species. Proceedings of the National Academy of Sciences of the United States of America. 107: 3982-7. PMID 20147623 DOI: 10.1073/Pnas.0911565107 |
0.374 |
|
2010 |
Grzyska PK, Hausinger RP, Proshlyakov DA. Metal and substrate binding to an Fe(II) dioxygenase resolved by UV spectroscopy with global regression analysis. Analytical Biochemistry. 399: 64-71. PMID 19932076 DOI: 10.1016/J.Ab.2009.11.022 |
0.3 |
|
2007 |
Grzyska PK, Hausinger RP. Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase. Inorganic Chemistry. 46: 10087-92. PMID 17973473 DOI: 10.1021/Ic700383Q |
0.311 |
|
2007 |
Zalatan JG, Catrina I, Mitchell R, Grzyska PK, O'brien PJ, Herschlag D, Hengge AC. Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis. Journal of the American Chemical Society. 129: 9789-98. PMID 17630738 DOI: 10.1021/Ja072196+ |
0.598 |
|
2007 |
Muthukumaran RB, Grzyska PK, Hausinger RP, McCracken J. Probing the iron-substrate orientation for taurine/alpha-ketoglutarate dioxygenase using deuterium electron spin echo envelope modulation spectroscopy. Biochemistry. 46: 5951-9. PMID 17469855 DOI: 10.1021/Bi700562T |
0.322 |
|
2007 |
Grzyska PK, Müller TA, Campbell MG, Hausinger RP. Metal ligand substitution and evidence for quinone formation in taurine/alpha-ketoglutarate dioxygenase. Journal of Inorganic Biochemistry. 101: 797-808. PMID 17350690 DOI: 10.1016/J.Jinorgbio.2007.01.011 |
0.385 |
|
2007 |
Grzyska PK, Czyryca PG, Purcell J, Hengge AC. Transition State Differences in Hydrolysis Reactions of Alkyl versus Aryl Phosphate Monoester Monoanions [J. Am. Chem. Soc.2003,125, 13106−13111]. Journal of the American Chemical Society. 129: 5298-5298. DOI: 10.1021/Ja071527F |
0.668 |
|
2006 |
Luo L, Pappalardi MB, Tummino PJ, Copeland RA, Fraser ME, Grzyska PK, Hausinger RP. An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation. Analytical Biochemistry. 353: 69-74. PMID 16643838 DOI: 10.1016/J.Ab.2006.03.033 |
0.407 |
|
2005 |
Kalliri E, Grzyska PK, Hausinger RP. Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase, TauD. Biochemical and Biophysical Research Communications. 338: 191-7. PMID 16165092 DOI: 10.1016/J.Bbrc.2005.08.223 |
0.357 |
|
2005 |
Grzyska PK, Ryle MJ, Monterosso GR, Liu J, Ballou DP, Hausinger RP. Steady-state and transient kinetic analyses of taurine/alpha-ketoglutarate dioxygenase: effects of oxygen concentration, alternative sulfonates, and active-site variants on the FeIV-oxo intermediate. Biochemistry. 44: 3845-55. PMID 15751960 DOI: 10.1021/Bi048746N |
0.46 |
|
2004 |
Grzyska PK, Kim Y, Jackson MD, Hengge AC, Denu JM. Probing the transition-state structure of dual-specificity protein phosphatases using a physiological substrate mimic. Biochemistry. 43: 8807-14. PMID 15236589 DOI: 10.1021/Bi049473Z |
0.697 |
|
2004 |
McCain DF, Grzyska PK, Wu L, Hengge AC, Zhang ZY. Mechanistic studies of protein tyrosine phosphatases YopH and Cdc25A with m-nitrobenzyl phosphate. Biochemistry. 43: 8256-64. PMID 15209522 DOI: 10.1021/Bi0496182 |
0.724 |
|
2003 |
Grzyska PK, Czyryca PG, Purcell J, Hengge AC. Transition state differences in hydrolysis reactions of alkyl versus aryl phosphate monoester monoanions. Journal of the American Chemical Society. 125: 13106-11. PMID 14570483 DOI: 10.1021/Ja036571J |
0.682 |
|
2002 |
Grzyska PK, Czyryca PG, Golightly J, Small K, Larsen P, Hoff RH, Hengge AC. Generality of solvation effects on the hydrolysis rates of phosphate monoesters and their possible relevance to enzymatic catalysis. The Journal of Organic Chemistry. 67: 1214-20. PMID 11846665 DOI: 10.1021/Jo016104P |
0.673 |
|
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