Publications by authors named "George E Cutsail Iii"

Oxidoreductases have evolved tyrosine/tryptophan pathways that channel highly oxidizing holes away from the active site to avoid damage. Here we dissect such a pathway in a bacterial LPMO, member of a widespread family of C-H bond activating enzymes with outstanding industrial potential. We show that a strictly conserved tryptophan is critical for radical formation and hole transference and that holes traverse the protein to reach a tyrosine-histidine pair in the protein's surface.

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The recent successes in the isolation and characterization of several bismuth radicals inspire the development of new spectroscopic approaches for the in-depth analysis of their electronic structure. Electron paramagnetic resonance (EPR) spectroscopy is a powerful tool for the characterization of main group radicals. However, the large electron-nuclear hyperfine interactions of Bi (Bi, = 9/2) have presented difficult challenges to fully interpret the spectral properties for some of these radicals.

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Pseudomonas putida rubredoxin-2 (Rxn2) is an essential member of the alkane hydroxylation pathway and transfers electrons from a reductase to the membrane-bound hydroxylase. The regioselective hydroxylation of linear alkanes is a challenging chemical transformation of great interest for the chemical industry. Herein, we report the preparation and spectroscopic characterization of cobalt-substituted P.

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