Abstract

The nature of metal binding sites in copper-containing proteins is being probed by chemical modification studies in combination with spectral investigations and by studies of synthetic model systems. The proteins being studied directly are azurin, stellacyanin, and laccase. Apoproteins, metal-replaced, and metal-substituted proteins are being prepared and characterized. In the case of azurin the kinetics of metal uptake by the peptide moiety is being examined in an effort to understand the basis of the kinetic selectivity which is expressed for Cu(II). Attempts to prepare liganded and mixed derivatives of laccase are being pursued to get at cooperative interactions among the metal binding sites. A small molecule system with an N2S2 donor set is being synthesized as a model of the type l site. Kinetic studies of amacrocyclic copper complex are also planned.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM022764-09S1
Application #
3271320
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1976-03-01
Project End
1985-11-30
Budget Start
1985-09-01
Budget End
1985-11-30
Support Year
9
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Purdue University
Department
Type
Schools of Arts and Sciences
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907

  Publications

Antholine, W E; Hanna, P M; McMillin, D R (1993) Low frequency EPR of Pseudomonas aeruginosa azurin. Analysis of ligand superhyperfine structure from a type 1 copper site. Biophys J 64:267-72
Li, J; McMillin, D R (1992) The removal of the type-2 copper from Rhus vernicifera laccase. Biochim Biophys Acta 1160:239-45
Klemens, F K; McMillin, D R (1992) Room-temperature phosphorescence from azurin derivatives. Phosphorescence quenching in oxidized native azurin. Photochem Photobiol 55:671-6
Lu, J; Bender, C J; McCracken, J et al. (1992) Pulsed EPR studies of the type 2 copper binding site in the mercury derivative of laccase. Biochemistry 31:6265-72
Meadows, K A; Morie-Bebel, M M; McMillin, D R (1991) Copper transfer from Rhus vernicifera laccase. J Inorg Biochem 41:253-60
Klemens, A S; McMillin, D R (1990) New method for removing type 2 copper from Rhus laccase. J Inorg Biochem 38:107-15
Severns, J C; McMillin, D R (1990) Temperature and anation studies of the type 2 site in Rhus vernicifera laccase. Biochemistry 29:8592-7
Tamilarasan, R; McMillin, D R (1989) Spectroscopic studies of the type 2 and type 3 copper centres in the mercury derivative of laccase. Biochem J 263:425-9
Byrd, J; Berger, R M; McMillin, D R et al. (1988) Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants. J Biol Chem 263:6688-94
Hanna, P M; Tamilarasan, R; McMillin, D R (1988) Cu(I) analysis of blue copper proteins. Biochem J 256:1001-4

Showing the most recent 10 out of 14 publications