Abstract

Proteins containing copper, molybdenum, and iron-sulfur clusters, which are involved in biological electron transport, hydrogen and nitrogen metabolism, and redox transformations of metabolites, will be studied with the aim of understanding the basis of activity in molecular structure. Resonance Raman spectroscopy will be utilized, to monitor the vibrational frequencies of the molecular entities at the protein active site, and the spectra will be analyzed with the aid of appropriate model compounds and normal coordinate calculations. EXAFS (extended x-ray absorption fine structure) analysis will be used to help characterize the structure and dynamics of copper proteins.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM013498-21
Application #
3268497
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1977-08-01
Project End
1989-07-31
Budget Start
1986-08-01
Budget End
1987-07-31
Support Year
21
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Princeton University
Department
Type
Schools of Arts and Sciences
DUNS #
002484665
City
Princeton
State
NJ
Country
United States
Zip Code
08544

  Publications

Spiro, Thomas G (2007) Adventures in bioinorganic chemistry. Inorg Chem 46:10968-80
Dong, S; Ybe, J A; Hecht, M H et al. (1999) H-bonding maintains the active site of type 1 copper proteins: site-directed mutagenesis of Asn38 in poplar plastocyanin. Biochemistry 38:3379-85
Qiu, D; Kumar, M; Ragsdale, S W et al. (1994) Nature's carbonylation catalyst: Raman spectroscopic evidence that carbon monoxide binds to iron, not nickel, in CO dehydrogenase. Science 264:817-9
Clements, A P; Kilpatrick, L; Lu, W P et al. (1994) Characterization of the iron-sulfur clusters in ferredoxin from acetate-grown Methanosarcina thermophila. J Bacteriol 176:2689-93
Madden, J F; Han, S H; Siegel, L M et al. (1989) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. Biochemistry 28:5471-7
Han, S H; Madden, J F; Thompson, R G et al. (1989) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry 28:5461-71
Han, S H; Madden, J F; Siegel, L M et al. (1989) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. Biochemistry 28:5477-85
Macor, K A; Czernuszewicz, R S; Adams, M W et al. (1987) An investigation of hydrogenase I and hydrogenase II from Clostridium pasteurianum by resonance Raman spectroscopy. Evidence for a [2Fe-2S] cluster in hydrogenase I. J Biol Chem 262:9945-7
Nestor, L; Reinhammar, B; Spiro, T G (1986) 63/65Cu and 1/2H2O isotope shifts in the low-temperature resonance Raman spectrum of fungal laccase. Biochim Biophys Acta 869:286-92