Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase.

Abstract

Phenylalanine hydroxylase is a mononuclear non-heme iron protein that uses tetrahydropterin as the source of the two electrons needed to activate dioxygen for the hydroxylation of phenylalanine to tyrosine. Rapid-quench methods have been used to analyze the mechanism of a bacterial phenylalanine hydroxylase from Chromobacterium violaceum. Mössbauer spectra… (More)
DOI: 10.1021/bi1019868

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Cite this paper

@article{Panay2011EvidenceFA, title={Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase.}, author={Aram Joel Panay and Michael Lee and Carsten Krebs and J. Martin Bollinger and Paul F Fitzpatrick}, journal={Biochemistry}, year={2011}, volume={50 11}, pages={1928-33} }