James D. Satterlee

Professor

Address

Fulmer 101
Pullman, WA 99164-4630

(509) 335-8620 / 5-6487
email: hemeteam@wsu.edu
personal page: http://www.wsu.edu/~hemeteam

Education

Research

Professor Satterlee came to WSU from the University of New Mexico in 1989. He completed undergraduate work at Central Washington University (1971) and obtained his Ph.D. at the University of California, Davis (1975), under the tutelage of Gerd La Mar. From 1975 to 1978 he was a research fellow at the California Institute of Technology, where he worked with John H. Richards. He was an Alfred P. Sloan Foundation Fellow from 1983 to 1987 and held a National Institutes of Health Research Career Development Award from 1988-1992.

Interests: (A) Heme Protein Chemistry; (B) Environmental Chemistry

(A) Heme Protein Chemistry

As our protein-group nickname implies, Hemeteam research focuses on the Chemistry and Biochemistry of Heme proteins. These proteins, all of which contain an iron porphyrin prosthetic group as their active site, are ubiquitous. Heme proteins display diverse magnetic and structural features that belie their function and provide ample Biophysical properties with which to study them. In nature heme proteins function in a variety of processes, including oxygen transport and storage, intracellular oxygen and iron trafficking, oxygen sensing, activation of oxygen-containing molecules, enzymatic transformations of organic molecules, NO synthesis and regulation, oxidative metabolism, electron transfer, cellular signaling, apoptosis and regulation of DNA expression.

Among the heme proteins currently being studied by the hemeteam are the following. 1) We study several species of oxygen sensing/signalling proteins that are structurally multi-domain, multi-functional, as well. The FixLs are the current focus of our work. They are sensing and signaling heme proteins that regulate expression of the genes required for nitrogen fixation. 2) Peroxidases are a class of enzymes that use metabolic hydrogen peroxide to catalyze chemical transformations and to carry out electron transfers; 3) Complexes between cytochrome c peroxidase and the c-type cytochromes are active in biological electron transfer and are easily studied using NMR spectroscopy.

Experimental approaches that we use include Biochemical, Chemical and Biophysical methods. As an illustration, the following list is a compilation of methods that the Hemeteam has used recently: protein isolation and purification, lplc, hplc, electophoresis, isoelectric focusing, uv-visible spectroscopy, infrared spectroscopy, mass spectrometry, 1D-4D NMR spectroscopy, magnetic relaxation, protein dynamics, fast and slow kinetics, cloning, protein expression, PCR, mutagenesis, molecular modeling, molecular dynamics simulations, mass spectrometry, solution structure determination, and crystal structure determination.

(B) Environmental Chemistry

Our lab has also started a small program designed to elucidate regional and national environmental problems. Recently we have begun gathering data on the wide-spread regional practice of post-harvest agricultural field burning. Data is being gathered on the particle densities associated with combustion smog in Pullman. We are also analyzing the smoke to determine its chemical constituents. Among the most plentiful chemicals found are various phenols, which are highly toxic, and several types of aromatic and polyaromatic hydrocarbons.

Please note that there are no graduate student positions open in my laboratory at this time.

Publications