Abstract

Metals or metalloids of primary importance to this study are cadmium and selenium. These nuclei are ideally suited for a multinuclear magnetic resonance study involving direct observation of the metal nucleus by Fourier transform techniques because of their respective receptiveness to an nmr experiment and because they are spin 1/2 nuclei. The principal objectives of this project can be divided into two broad categories. First, we will be involved in detailed studies of the mode of interactions of cadmium with metalloproteins. The systems of particular interest to us here are cadmium substituted concanavalin-A, bovine superoxide dismutase, and carboxy-peptidase-A. Secondly, a study of the utility of 77Se nmr in biological systems will be initiated. The proposed 77Se nmr research is further subdivided into three areas of interest. These areas include: (1) the elucidation of the mechanism of the oxidation of sulfhydryl groups by selenium compounds, (2) an effort to clarify the metabolic interactions of selenium with other elements of ecologic concern, i.e. cadmium, mercury, and arsenic, (3) a general survey will be conducted of the molecular identity of selenium within accumulator plants and various bacteria.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM026295-06
Application #
3273793
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1979-04-01
Project End
1985-11-30
Budget Start
1984-12-01
Budget End
1985-11-30
Support Year
6
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of South Carolina at Columbia
Department
Type
Schools of Arts and Sciences
DUNS #
111310249
City
Columbia
State
SC
Country
United States
Zip Code
29208

  Publications

Lipton, Andrew S; Bergquist, Catherine; Parkin, Gerard et al. (2003) Solid-State 67Zn NMR spectroscopic studies and ab initio molecular orbital calculations on a synthetic analogue of carbonic anhydrase. J Am Chem Soc 125:3768-72
Lipton, Andrew S; Wright, Terri A; Bowman, Michael K et al. (2002) Solid-state (67)zn NMR spectroscopy in bioinorganic chemistry. Spectra of four- and six-coordinate zinc pyrazolylborate complexes obtained by management of proton relaxation rates with a paramagnetic dopant. J Am Chem Soc 124:5850-60
Lipton, Andrew S; Smith, Mark D; Adams, Richard D et al. (2002) 67Zn solid-state and single-crystal NMR spectroscopy and X-ray crystal structure of zinc formate dihydrate. J Am Chem Soc 124:410-4
Lipton, A S; Buchko, G W; Sears, J A et al. (2001) 67Zn solid-state NMR spectroscopy of the minimal dna binding domain of human nucleotide excision repair protein XPA. J Am Chem Soc 123:992-3
Lipton, A S; Sears, J A; Ellis, P D (2001) A general strategy for the NMR observation of half-integer quadrupolar nuclei in dilute environments. J Magn Reson 151:48-59
McAteer, K; Lipton, A S; Kennedy, M A et al. (1996) A multiphase 113Cd NMR investigation of metalloporphyrin reorientation in cadmium-substituted myoglobin. Solid State Nucl Magn Reson 7:229-38
Koons, J M; Ellis, P D (1995) Applicability of factor analysis in solid state NMR. Anal Chem 67:4309-15
Ellis, P D (1989) 113Cd NMR of Cd2+-substituted carboxypeptidase. Support for a hexa-coordinate metal ion in the presence of inhibitors. J Biol Chem 264:3108-10
Ellis, P D; Marchetti, P S; Strang, P et al. (1988) Cadmium-substituted skeletal troponin C metal binding investigations and sequence assignment of the cadmium-113 resonances. J Biol Chem 263:10284-8
Bhattacharyya, L; Marchetti, P S; Ellis, P D et al. (1987) Nuclear magnetic resonance investigation of cadmium 113 substituted pea and lentil lectins. J Biol Chem 262:5616-21

Showing the most recent 10 out of 11 publications