Metalloproteins thin films

Author

Margalit, Ruth ; Vasquez, Richard P.

Author_Institution

Jet Propulsion Lab., California Inst. of Technol., Padadena, CA, USA

fYear

1989

fDate

9-12 Nov 1989

Firstpage

1315

Abstract

The structure and orientation of metalloproteins adsorbed onto semiconductor and metal surfaces were investigated. X-ray photoelectron spectroscopy (XPS) techniques were used in conjunction with novel myoglobin derivatives. In these myoglobin derivatives, a pentammine ruthenium (III) group is attached to specific histidine residues on the protein surface. The Fe-Ru distance in these derivatives was calculated and found to be on the order of 13-25 Å. Measurements of the intensity ratio of the Ru 3p_3/2 or Ru 3d_5/2 to Fe 2p_3/2 XPS peaks provide an indicator of the degree of ordering in the film

Keywords

X-ray photoelectron spectra; molecular biophysics; proteins; Fe-Ru distance; X-ray photoelectron spectroscopy; degree of ordering; histidine residues; intensity ratio; metal surfaces; metalloproteins thin films; myoglobin derivatives; orientation; pentammine ruthenium group; protein surface; semiconductor surfaces; structure; Amino acids; Biological control systems; Biological materials; Iron; Laboratories; Molecular electronics; Proteins; Semiconductor thin films; Substrates; Transistors;

fLanguage

English

Publisher

ieee

Conference_Titel

Engineering in Medicine and Biology Society, 1989. Images of the Twenty-First Century., Proceedings of the Annual International Conference of the IEEE Engineering in

Conference_Location

Seattle, WA

Type

conf

DOI

10.1109/IEMBS.1989.96213

Filename

96213