A Hot Oxidant, 3-NO₂Y₁₂₂ Radical, Unmasks Conformational Gating in Ribonucleotide Reductase

DOI: 10.1021/ja1069344 Authors: Kenichi Yokoyama, Ulla Uhlin, JoAnne Stubbe Abstract: Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides and requires a diferric-tyrosyl radical (Y(•)) cofactor...

Reduction and Oxidation of the Active Site Iron in Tyrosine Hydroxylase:  Kinetics and Specificity

DOI: 10.1021/bi052283j Authors: Patrick A. Frantom, Javier Seravalli, Stephen W. Ragsdale, Paul F. Fitzpatrick Abstract: Tyrosine hydroxylase (TyrH) is a pterin-dependent enzyme that catalyzes the hydroxylation of tyrosine to form dihydroxyphenylalanine. The oxidation...

Pre-steady-state Kinetic Analysis of Recombinant Arabidopsis NADH:Nitrate Reductase

DOI: 10.1074/jbc.m100356200 Authors: Lawrie Skipper, Wilbur Campbell, Jeffrey A. Mertens, David J. Lowe Abstract: Recombinant Arabidopsis NADH:nitrate reductase was expressed in Pichia pastoris using fermentation. Large enzyme quantities were purified for...

Characterization of Y122F R2 of Escherichia coli Ribonucleotide Reductase by Time-Resolved Physical Biochemical Methods and X-ray Crystallography^,

DOI: 10.1021/bi9728811 Authors: Wing H. Tong, Doug Burdi, P. Riggs-Gelasco, S. Chen, Dale E. Edmondson, B.H. Huynh, J. Stubbe, Seungil Han, A.S. Arvai, John A. Tainer Abstract: Ribonucleotide reductase (RNR) from Escherichia coli catalyzes the conversion of...

Reactivity of Deoxy- and Oxyferrous Dehaloperoxidase B from Amphitrite ornata: Identification of Compound II and Its Ferrous–Hydroperoxide Precursor

DOI: 10.1021/bi200311u Authors: Jennifer D’Antonio, Reza A. Ghiladi Abstract: Dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata is a bifunctional enzyme that possesses both hemoglobin and peroxidase activities. The bifunctional nature of DHP as a...