The purpose of the propsed research is to elucidate the biochemistry, physiology, and structure of new coenzymes and vitamins that have been discovered in methanogenic bacteria. In the history of biochemistry, microbbes have played a pivitol role in the assay of viatamins as well as in the elucidation of the biochemical function of vitamins and coenzymes. To completely understand cell chemistry is important, for biochemical deficiencies produce a diseased state. Study of methanogens have revealed 7 new factor-coenzyme relationships. Study of these coenzymes is providing new insights into biochemical reactions. To study these coenzymes methanogens are mass cultered in kilogram quantities on H2 + CO2. Coenzymes are frationated from cell extracts to homogeniety, and their structure is then determined by use of mass spectrometry, 1H-NMR, 13C-NMR, elemental analysis and other analytical procedures. The biochemical role of each coenzyme in enzymatic catalysis is studied theough purification of the enzymes that requires the coenzyme for catalytic activity. Methanogens are only distantly related to typical bacteria, and because of their unusual metabolism are providing unique handles by processing certain coenzymes in unusually high concentrations.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI012277-15
Application #
3125150
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1974-09-01
Project End
1989-08-31
Budget Start
1988-09-01
Budget End
1989-08-31
Support Year
15
Fiscal Year
1988
Total Cost
Indirect Cost
Name
University of Illinois Urbana-Champaign
Department
Type
Schools of Arts and Sciences
DUNS #
041544081
City
Champaign
State
IL
Country
United States
Zip Code
61820
Kuhner, C H; Lindenbach, B D; Wolfe, R S (1993) Component A2 of methylcoenzyme M reductase system from Methanobacterium thermoautotrophicum delta H: nucleotide sequence and functional expression by Escherichia coli. J Bacteriol 175:3195-203
Woo, G J; Wasserfallen, A; Wolfe, R S (1993) Methyl viologen hydrogenase II, a new member of the hydrogenase family from Methanobacterium thermoautotrophicum delta H. J Bacteriol 175:5970-7
Olson, K D; Chmurkowska-Cichowlas, L; McMahon, C W et al. (1992) Structural modifications and kinetic studies of the substrates involved in the final step of methane formation in Methanobacterium thermoautotrophicum. J Bacteriol 174:1007-12
Reddy, D M; Crain, P F; Edmonds, C G et al. (1992) Structure determination of two new amino acid-containing derivatives of adenosine from tRNA of thermophilic bacteria and archaea. Nucleic Acids Res 20:5607-15
Kuhner, C H; Smith, S S; Noll, K M et al. (1991) 7-Mercaptoheptanoylthreonine phosphate substitutes for heat-stable factor (mobile factor) for growth of Methanomicrobium mobile. Appl Environ Microbiol 57:2891-5
Olson, K D; McMahon, C W; Wolfe, R S (1991) Light sensitivity of methanogenic archaebacteria. Appl Environ Microbiol 57:2683-6
Olson, K D; McMahon, C W; Wolfe, R S (1991) Photoactivation of the 2-(methylthio)ethanesulfonic acid reductase from Methanobacterium. Proc Natl Acad Sci U S A 88:4099-103
Bobik, T A; DiMarco, A A; Wolfe, R S (1990) Formyl-methanofuran synthesis in Methanobacterium thermoautotrophicum. FEMS Microbiol Rev 7:323-6
Jablonski, P E; DiMarco, A A; Bobik, T A et al. (1990) Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila. J Bacteriol 172:1271-5
DiMarco, A A; Sment, K A; Konisky, J et al. (1990) The formylmethanofuran:tetrahydromethanopterin formyltransferase from Methanobacterium thermoautotrophicum delta H. Nucleotide sequence and functional expression of the cloned gene. J Biol Chem 265:472-6

Showing the most recent 10 out of 33 publications