Abstract

Blue copper proteins function as mobile electron carriers in biological systems by transfering electrons to and from their "type I" copper active sites liganded to the protein matrix.¹ In reduced form, these active sites have a strong ligand-to-metal charge transfer transition between the copper atom and a cysteine sulfur ligand in the region of 595-630 nm, which gives the proteins their characterisitic blue color.² This strong absorption makes blue copper proteins suitable for ultrafast spectroscopic studies of protein electron transfer. Elucidation of electronic and nuclear dynamics of these systems requires classical and quantum simulations in conjunction with experiment. The resultant spectral density describing the optically induced charge transfer process may be useful in understanding the long range electron transfer of physiological function.

© 1996 Optical Society of America