J. Phys. IV France
Volume 7, Numéro C2, Avril 1997
Proceedings of the 9th International Conference on X-Ray Absorption Fine Structure
Page(s) C2-593 - C2-597
Proceedings of the 9th International Conference on X-Ray Absorption Fine Structure

J. Phys. IV France 7 (1997) C2-593-C2-597

DOI: 10.1051/jp4/1997108

XAFS on Vectorially-Oriented Single Monolayer Protein Samples

K. Zhang1, A. M. Edwards2, J. Dong1, J. Chupa2 and J. K. Blasie2

1  Illinois Institute of Technology, Chicago, IL 60616, University City Science Center, Philadelphia, PA 19104, U.S.A.
2  Department ofChemistry, University of Pennsylvania, Philadelphia, PA 19104, U.S.A.

Polarized XAFS measurements were carried out on a single monolayer of cytochrome c tethered to a self assembled organic monolayer. The monolayer contains 1012 to 1013 protein molecules per cm2, which is 10 to 100 times more dilute than a single monolayer of small inorganic molecules. Thus, the spectra were collected under total reflection conditions to ensure a reasonable signal to noise ratio by increasing signal counts and, in the mean time, reducing background. The.spectrum with X-ray polarization parallel to the substrate surface is found to be similar to the spectrum'of the perpendicular orientation. However, the spectra are somewhat different from the spectrum of cytochrome c in a frozen solution. The differences may be attributed to thermal effects and/or the impurity signal from the silicon or quartz substrates. Optical linear dichroism measurements determined the tilt angle between the average heme-plane and the substrate surface plane to be about 40°, consistent with XAFS observations. XAFS experiments on a single protein monolayer provide new opportunities for probing metal centers in biology.

© EDP Sciences 1997