Mononuclear copper monooxygenases catalyze physiological reactions critical for hormone and neurotransmitter processing. These enzymes employ long-distance electron transfer between two copper active sites. We have conducted extensive electronic structure analysis of the α-hydroxylating monooxygenase active sites using hybrid DFT methods. Our studies identify electronic structure features of the copper active sites and nearby residues that are critical for the electron transfer function. We employed state of art DFT approaches to compute the inter-domain electronic coupling interactions and other significant electronic properties of the enzyme. Our analysis develops protocols for choosing appropriate QM regions in the QM/MM calculations needed to estimate the electron transfer rates.

Modeling inter-domain electron tunneling in copper monooxygenases

249th National Meeting (2015)

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