Abstract
Phenylalanine hydroxylase (PAH) from Chromobacterium violaceum (CV) is known to bind an equivalent of divalent copper.1 Studies using pulsed EPR spectroscopy2 have suggested that there are two equatorial imidazoles coordinated to Cu(II) of CV PAH. This observation has been supported by copper-histidine model complexes of the active site3 and more recently by X-ray absorption spectroscopy of the copper containing enzyme.4 We have used a combination of site directed mutagenesis and pulsed EPR spectroscopy to probe the copper binding site of CV PAH and identify the Cu(II) ligands.
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