Electron transfer from gold nanoparticle cores to cytochrome c in self-organized protein superstructures

INOR 429

Amanda S. Harper-Leatherman, aharper@mail.fairfield.edu1, Alex N. Capecelatro, acaps@ucla.edu2, Christopher P. Rhodes2, Jeffrey W. Long2, and Debra R. Rolison2. (1) Department of Chemistry, Fairfield University, 1073 North Benson Road, Fairfield, CT 06824, (2) Surface Chemistry Branch, Naval Research Laboratory, Code 6170, 4555 Overlook Avenue SW, Washington, 20375
We recently reported the encapsulation of heme protein superstructures within ultraporous aerogels that demonstrated rapid response for binding gas-phase nitric oxide. The protein superstructures, nucleated in buffered media by colloidal gold nanoparticles, protect cytochrome c to the extent that the protein survives the harsh physical and chemical processing conditions necessary to form the silica aerogel nanoarchitecture. We are interested in the potential application of these biomolecular composite aerogels, but we have also chosen to explore the fundamental properties of the superstructures in buffered media, outside of the aerogel nanoarchitecture, in order to further our understanding of these stabilizing superstructures. We will present UV-vis, Raman, and X-ray photoelectron spectroscopic data that provide evidence that the gold-nucleated protein superstructure is a dynamic structure in which the proteins can rearrange and perform electron transfer, perhaps in a similar way to what occurs in the cell.
 

Nanoscience: Synthesis and Characterization
2:00 PM-5:20 PM, Monday, August 20, 2007 BCEC -- 209, Oral

Division of Inorganic Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007