The mammalian vision system contains a complex array of proteins involved in signaling, transport, and other functions. Several of these proteins have been shown to be metalloenzymes, including RPE65, a membrane-bound iron-dependent enzyme that regenerates the essential visual chromophore 11-cis-retinal, and DNPEP, a zinc-dependent aspartyl aminopeptidase thought to be involved in peptide signaling regulation in the eye. A number of fundamental questions regarding the function of these enzymes remain unaddressed, such as the precise role of the iron center in RPE65. We will present recent progress from our X-ray absorption spectroscopy (XAS) studies of RPE65 and DNPEP, complementing existing data from  macromolecular crystallography and enzymology. The significance of our spectroscopic data in relation to postulated enzyme function will be discussed.

Structural insights from X-ray absorption spectroscopy into metalloenzymes involved in mammalian vision

244th National Meeting (2012)

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