Abstract

The proposed project will determine structural elements for the enzyme responsible for nitrite reduction in dissimilatory denitrification. Proton nuclear magnetic resonance spectroscopy will be used to determine structure about the catalytic site heme groups, including the characterization of electronic states. Resonance raman spectroscopy will be used to investigate the vibrational states of the catalytic sites. The exact chemical structure of the prosthetic groups of the enzyme will be determined by purification of these from the intact enzyme and a structural determination through nuclear magnetic resonance, vibrational, optical, and mass spectroscopy. The interactions of oxides of nitrogen with whole cells will also be examined. The target enzyme system is representative of the general class of electron transport enzymes and proteins. Its study will promote the understanding on a fundamental level of this class which is responsible for energy production and respiration in all cells.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM036264-04
Application #
3289890
Study Section
Biochemistry Study Section (BIO)
Project Start
1985-07-01
Project End
1990-04-30
Budget Start
1988-05-01
Budget End
1989-04-30
Support Year
4
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
University of Alabama in Tuscaloosa
Department
Type
Schools of Arts and Sciences
DUNS #
City
Tuscaloosa
State
AL
Country
United States
Zip Code
35487

  Publications

Qabar, A N; Stern, M S; Walz, D A et al. (1991) Hierarchy of globin complexes. The quaternary structure of the extracellular chlorocruorin of Eudistylia vancouverii. J Mol Biol 222:1109-29
Yap-Bondoc, F; Timkovich, R (1990) Inactivation of cytochrome cd1 by hydrazines. J Biol Chem 265:4247-53
Andersson, L A; Loehr, T M; Wu, W S et al. (1990) Modelling heme d1. The spectral properties of copper(II) porphyrindiones. FEBS Lett 267:285-8
Timkovich, R (1990) 15N NMR spectroscopy of Pseudomonas cytochrome c-551. Biochemistry 29:7773-80
Yap-Bondoc, F; Bondoc, L L; Timkovich, R et al. (1990) C-methylation occurs during the biosynthesis of heme d1. J Biol Chem 265:13498-500
Chau, M H; Cai, M L; Timkovich, R (1990) NMR comparison of prokaryotic and eukaryotic cytochromes c. Biochemistry 29:5076-87
Bondoc, L L; Timkovich, R (1989) Structural characterization of nitrimyoglobin. J Biol Chem 264:6134-45
Timkovich, R; Thrasher, J S (1988) Carbon monoxide oxygenase activity of cytochrome cd1. Biochemistry 27:5383-8
Timkovich, R; Cai, M L; Dixon, D W (1988) Electron self-exchange in Pseudomonas cytochromes. Biochem Biophys Res Commun 150:1044-50
Jones, K H; Lindahl, R; Baker, D C et al. (1987) Hydride transfer stereospecificity of rat liver aldehyde dehydrogenases. J Biol Chem 262:10911-3

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