Abstract

This project seeks to understand the molecular interactions whereby proteins control the activity of imbedded metal ions, which are known to carry out key biochemical reactions, including electron transfer an oxygen activation. Systems of interest include the iron-sulfur class of proteins, copper proteins, molybdenum proteins, and vanadium proteins. Resonance Raman spectroscopy is used to probe structural details of the active sites in important functional states. Further development of the method to increase its utility is an essential part of the program.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM013498-32
Application #
2684622
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1977-08-01
Project End
2001-03-31
Budget Start
1998-04-01
Budget End
2001-03-31
Support Year
32
Fiscal Year
1998
Total Cost
Indirect Cost

  Institution

Name
Princeton University
Department
Chemistry
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
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
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
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