Abstract

Mossbauer and EPR studies of hydrogenases isolated from Clostridium pasteurianum W5 and from sulfate reducing bacteria are proposed. Hydrogenase is capable of activating molecular hydrogen and many micro-organisms use it to metabolize H2. Understanding the hydrogenase mechanism could be a key step toward catalysis of hydrogen production from water and solar energy, a potentially important alternate energy source. Despite the importance of its biological functions, hidrogenase is poorly understood. The proposed studies should reveal physical properties and structural information pertinent to the prosthetic groups of hydrogenase; information essential to the understanding of its catalytic mechanism. Our preliminary studies have acquired evidence against the present understanding of a HiPIP center in C. pasteurianum hydrogenase, and have established unambiguously the presence of a redox-active nickel center in hydrogenases form Desulfovibrio gigas and Desulfovibrio desulfuricans. Since nickel has only been recently recognized as an important trace element in biological systems. Our studies will be undoubtedly an important step toward the understanding of biological functions of nickel in proteins.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM032187-02
Application #
3280794
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1983-12-01
Project End
1986-11-30
Budget Start
1984-12-01
Budget End
1985-11-30
Support Year
2
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Emory University
Department
Type
Schools of Arts and Sciences
DUNS #
042250712
City
Atlanta
State
GA
Country
United States
Zip Code
30322

  Publications

Barata, B A; Liang, J; Moura, I et al. (1992) Mossbauer study of the native, reduced and substrate-reacted Desulfovibrio gigas aldehyde oxido-reductase. Eur J Biochem 204:773-8
Moura, I; Tavares, P; Moura, J J et al. (1992) Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774) J Biol Chem 267:4489-96
Ravi, N; Moura, I; Costa, C et al. (1992) Mossbauer characterization of the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743). Spectral deconvolution of the heme components. Eur J Biochem 204:779-82
Bollinger Jr, J M; Edmondson, D E; Huynh, B H et al. (1991) Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science 253:292-8
Lampreia, J; Moura, I; Teixeira, M et al. (1990) The active centers of adenylylsulfate reductase from Desulfovibrio gigas. Characterization and spectroscopic studies. Eur J Biochem 188:653-64
Moura, I; Tavares, P; Moura, J J et al. (1990) Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center. J Biol Chem 265:21596-602
Teixeira, M; Moura, I; Fauque, G et al. (1990) The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mossbauer characterization. Eur J Biochem 189:381-6
He, S H; Teixeira, M; LeGall, J et al. (1989) EPR studies with 77Se-enriched (NiFeSe) hydrogenase of Desulfovibrio baculatus. Evidence for a selenium ligand to the active site nickel. J Biol Chem 264:2678-82
Patil, D S; He, S H; DerVartanian, D V et al. (1988) The relationship between activity and the axial g = 2.06 EPR signal induced by CO in the periplasmic (Fe) hydrogenase from Desulfovibrio vulgaris. FEBS Lett 228:85-8
Patil, D S; Moura, J J; He, S H et al. (1988) EPR-detectable redox centers of the periplasmic hydrogenase from Desulfovibrio vulgaris. J Biol Chem 263:18732-8

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