Matthew J. Ryle
University of Michigan–Ann Arbor(US)Michigan State University(US)
Publications by Year
Research Areas
Metal-Catalyzed Oxygenation Mechanisms, Metalloenzymes and iron-sulfur proteins, Microbial metabolism and enzyme function, Heme Oxygenase-1 and Carbon Monoxide, Trace Elements in Health
Most-Cited Works
- → Direct Detection of Oxygen Intermediates in the Non-Heme Fe Enzyme Taurine/α-Ketoglutarate Dioxygenase(2004)296 cited
- → X-ray Crystal Structure of Escherichia coli Taurine/α-Ketoglutarate Dioxygenase Complexed to Ferrous Iron and Substrates,(2002)225 cited
- → Non-heme iron oxygenases(2002)210 cited
- → Stopped-Flow Kinetic Analysis ofEscherichia coliTaurine/α-Ketoglutarate Dioxygenase: Interactions with α-Ketoglutarate, Taurine, and Oxygen(1999)133 cited
- → O2- and α-Ketoglutarate-Dependent Tyrosyl Radical Formation in TauD, an α-Keto Acid-Dependent Non-Heme Iron Dioxygenase(2003)108 cited
- → Alternative Reactivity of an α-Ketoglutarate-Dependent Iron(II) Oxygenase: Enzyme Self-Hydroxylation(2001)94 cited
- → MgATP-Bound and Nucleotide-Free Structures of a Nitrogenase Protein Complex between the Leu 127Δ-Fe-Protein and the MoFe-Protein,(2000)90 cited
- → Elucidation of a MgATP Signal Transduction Pathway in the Nitrogenase Iron Protein: Formation of a Conformation Resembling the MgATP-Bound State by Protein Engineering(1996)75 cited
- → Steady-State and Transient Kinetic Analyses of Taurine/α-Ketoglutarate Dioxygenase: Effects of Oxygen Concentration, Alternative Sulfonates, and Active-Site Variants on the FeIV-oxo Intermediate(2005)73 cited
- → Nucleotide Hydrolysis and Protein Conformational Changes in Azotobacter vinelandii Nitrogenase Iron Protein: Defining the Function of Aspartate 129(1995)65 cited