Brenda A. Ley

O2 ACTIVATION BY NON-HEME DIIRON PROTEINS : IDENTIFICATION OF A SYMMETRIC MU -1,2-PEROXIDE IN A MUTANT OF RIBONUCLEOTIDE REDUCTASE

Mechanism of Rapid Electron Transfer during Oxygen Activation in the R2 Subunit of Escherichia coli Ribonucleotide Reductase. 1. Evidence for a Transient Tryptophan Radical

ENGINEERING THE DIIRON SITE OF ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE PROTEIN R2 TO ACCUMULATE AN INTERMEDIATE SIMILAR TO HPEROXO, THE PUTATIVE PER OXODIIRON(III) COMPLEX FROM THE METHANE MONOOXYGENASE CATALYTIC CYCLE

Rational Reprogramming of the R2 Subunit of Escherichia coli Ribonucleotide Reductase into a Self-Hydroxylating Monooxygenase

Mechanism of Rapid Electron Transfer during Oxygen Activation in the R2 Subunit of Escherichia coli Ribonucleotide Reductase. 2. Evidence for and Consequences of Blocked Electron Transfer in the W48F Variant

Crystal structure of the ribonucleotide reductase R2 mutant that accumulates a μ-1,2-peroxodiiron(III) intermediate during oxygen activation

Electron injection through a specific pathway determines the outcome of oxygen activation at the diiron cluster in the F208Y mutant of Escherichia coli ribonucleotide reductase protein R2.

Differential Iron(II) Affinity of the Sites of the Diiron Cluster in Protein R2 of Escherichia coli Ribonucleotide Reductase: Tracking the Individual Sites through the O2 Activation Sequence

Spectroscopic and Electronic Structure Description of the Reduced Binuclear Non-Heme Iron Active Site in Ribonucleotide Reductase fromE.coli: Comparison to Reduced Δ9Desaturase and Electronic Structure Contributions to Differences in O2Reactivity

Use of a Chemical Trigger for Electron Transfer to Characterize a Precursor to Cluster X in Assembly of the Iron-Radical Cofactor of Escherichia coli Ribonucleotide Reductase†