The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)
American Journal of Bioscience and Bioengineering
Volume 2, Issue 1, February 2014, Pages: 1-7
Received: Nov. 14, 2013; Published: Dec. 30, 2013
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Saidu Haruna, Department of Biological Sciences, Gombe State University, Gombe, Nigeria
Hamzat Ibiyeye Tijani, Department of Biochemistry, Bauchi State University Gadau, Bauchi, Nigeria
Yusuf Hindatu, Faculty of Bioscience & Medical Engineering, Universiti Teknologi Malaysia, 81310 Skudai, Johor-bahru, Malaysia
Jibrin Ndejiko Mohammed, Department of Microbiology, Ibrahim Badamasi Babangida University Lapai, Niger, Nigeria
Bashir Mohammed Abubakar, Department of Biological Sciences, Bauchi State University Gadau, Bauchi, Nigeria
Mohammed Sulaiman, Department of Biological Sciences, Gombe State University, Gombe, Nigeria
Abdulrahman Idris, Department of Microbiology, Kaduna State University, Kaduna, Nigeria
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Sulfate-reducing bacteria are categories of bacteria and archaea that can obtain energy by oxidizing organic compounds or molecular hydrogen (H2) while reducing sulfate (SO42−) to hydrogen sulfide (H2S). By analysis, these organisms "respire" sulfate rather than oxygen, a form of anaerobic respiration, the oxidation of hydrogen by the primary genus of Sulfate Reducing Bacteria (Desulfovibrio, Desulfovibrio desulfuricans) is catalyzed by enzymes called Hydrogenases. Three basic types of hydrogenases have been widely isolated from the primary genus of sulfate-reducing bacteria Desulfobibrio which differ in their structural subunits, metal compositions, physico-chemical characteristics, amino acid sequences, immunological activities, structural gene configuration and their catalytic properties. Broadly, hydrogenases can be considered as ‘iron containing hydrogenases and nickel-containing hydrogenases. The iron-sulfur-containing hydrogenase enzyme contains two ferredoxin-type (4Fe-4S) clusters and typical iron-sulfur center believed to be involved in the activation of H2 yet it is the most sensitive domain to CO and NO2−.eventhough it is not featured in all species of genus Desulfovibrio. The nickel-(iron-sulfur)-containing hydrogenases, [NiFe] hydrogenase posses two 4Fe-4S centers and one 3Fe-xS cluster in addition to nickel and have been found in all species of Desulfovibrio with strong resistance to CO and NO2- so far investigated. The genes encoding the large and small subunits of a periplasmic and membrane-bound species of the [NiFe] hydrogenase have been cloned in Escherichia coli and sequenced, however the functional complexity of the hydrogenase system remained unexplored as a result of the metabolic diversity in Desulfovibrio spp. The [NiFe] hydrogenase plays an important role in the energy metabolism of Desulfovibrio spp. Thus, the expression of the encoded structural genes would be an excellent marker for the metabolic functionalities under specific inducible environment.
Hydrogenases, Sulfate-Reducing Bacteria, Iron-Containing Hydrogenases, Genus: Desulfovibrio, Nickel-Iron-Containing-Hydrogenases, Nickel-Iron-Selenium-Containing Hydrogenases
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Saidu Haruna, Hamzat Ibiyeye Tijani, Yusuf Hindatu, Jibrin Ndejiko Mohammed, Bashir Mohammed Abubakar, Mohammed Sulaiman, Abdulrahman Idris, The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp), American Journal of Bioscience and Bioengineering. Vol. 2, No. 1, 2014, pp. 1-7. doi: 10.11648/
Carepo, M., J. Baptista, A. Pamplona, G. Fauque, J. Moura, and M. Reis, Hydrogen metabolism in< i> Desulfovibrio desulfuricans strain New Jersey (NCIMB 8313)—comparative study with< i> D. vulgaris and< i> D. gigas species. Anaerobe, 2002. 8(6): p. 325-332.
Volbeda, A., M.-H. Charon, C. Piras, E.C. Hatchikian, M. Frey, and J.C. Fontecilla-Camps, Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas. 1995.
Pereira, I.A.C., Respiratory membrane complexes of Desulfovibrio, in Microbial Sulfur Metabolism. 2008, Springer. p. 24-35.
Traore, A.S., C.E. Hatchikian, J. Le Gall, and J.-P. Belaich, Microcalorimetric studies of the growth of sulfate-reducing bacteria: comparison of the growth parameters of some Desulfovibrio species. Journal of bacteriology, 1982. 149(2): p. 606-611.
Odom, J. and H. Peck, Hydrogen cycling as a general mechanism for energy coupling in the sulfate‐reducing bacteria, Desulfovibrio sp. FEMS Microbiology Letters, 1981. 12(1): p. 47-50.
Peck, H.D., J. LeGall, P.A. Lespinat, Y. Berlier, and G. Fauque, A direct demonstration of hydrogen cycling by< i> Desulfovibrio vulgaris employing membrane-inlet mass spectrometry. FEMS microbiology letters, 1987. 40(2): p. 295-299.
Noguera, D.R., G.A. Brusseau, B.E. Rittmann, and D.A. Stahl, A unified model describing the role of hydrogen in the growth of Desulfovibrio vulgaris under different environmental conditions. Biotechnology and bioengineering, 1998. 59(6): p. 732-746.
LeGall, J. and G. Fauque, Dissimilatory reduction of sulfur compounds. Biology of anaerobic microorganisms, 1988: p. 587-639.
Volbeda, A., E. Garcin, C. Piras, A.L. de Lacey, V.M. Fernandez, E.C. Hatchikian, M. Frey, and J.C. Fontecilla-Camps, Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands⊥. Journal of the American Chemical Society, 1996. 118(51): p. 12989-12996.
Wawer, C., M. Jetten, and G. Muyzer, Genetic diversity and expression of the [NiFe] hydrogenase large-subunit gene of Desulfovibrio spp. in environmental samples. Applied and environmental microbiology, 1997. 63(11): p. 4360-4369.
Eidsness, M.K., R.A. Scott, B.C. Prickril, D.V. DerVartanian, J. Legall, I. Moura, J. Moura, and H.D. Peck, Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe] hydrogenases from Desulfovibrio baculatus. Proceedings of the National Academy of Sciences, 1989. 86(1): p. 147-151.
Garcin, E., X. Vernede, E. Hatchikian, A. Volbeda, M. Frey, and J. Fontecilla-Camps, The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure, 1999. 7(5): p. 557-566.
Przybyla, A.E., J. Robbins, N. Menon, and H.D. Peck Jr, Structure-function relationships among the nickel-containing hydrogenases. FEMS Microbiology Letters, 1992. 88(2): p. 109-135.
Thauer, R.K., Biochemistry of methanogenesis: a tribute to Marjory Stephenson: 1998 Marjory Stephenson Prize Lecture. Microbiology, 1998. 144(9): p. 2377-2406.
Fontecilla-Camps, J.C., A. Volbeda, C. Cavazza, and Y. Nicolet, Structure/function relationships of [NiFe]-and [FeFe]-hydrogenases. Chemical reviews, 2007. 107(10): p. 4273-4303.
Heidelberg, J.F., R. Seshadri, S.A. Haveman, C.L. Hemme, I.T. Paulsen, J.F. Kolonay, J.A. Eisen, N. Ward, B. Methe, and L.M. Brinkac, The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Nature biotechnology, 2004. 22(5): p. 554-559.
Huynh, B.H., M.H. Czechowski, H.-J. Krüger, D.V. DerVartanian, H.D. Peck, and J. LeGall, Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra. Proceedings of the National Academy of Sciences, 1984. 81(12): p. 3728-3732.
Valente, F.M., C.C. Almeida, I. Pacheco, J. Carita, L.M. Saraiva, and I.A. Pereira, Selenium is involved in regulation of periplasmic hydrogenase gene expression in Desulfovibrio vulgaris Hildenborough. Journal of bacteriology, 2006. 188(9): p. 3228-3235.
Matias, P.M., C.M. Soares, L.M. Saraiva, R. Coelho, J. Morais, J. Le Gall, and M.A. Carrondo, [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 Å and modelling studies of its interaction with the tetrahaem cytochrome c 3. JBIC Journal of Biological Inorganic Chemistry, 2001. 6(1): p. 63-81.
Volbeda, A., L. Martin, C. Cavazza, M. Matho, B.W. Faber, W. Roseboom, S.P. Albracht, E. Garcin, M. Rousset, and J.C. Fontecilla-Camps, Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases. JBIC Journal of Biological Inorganic Chemistry, 2005. 10(3): p. 239-249.
Higuchi, Y., T. Yagi, and N. Yasuoka, Unusual ligand structure in Ni–Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure, 1997. 5(12): p. 1671-1680.
Chiou, T.-W. and W.-F. Liaw, Nickel–thiolate and iron–thiolate cyanocarbonyl complexes: Modeling the nickel and iron sites of [NiFe] hydrogenase. Comptes Rendus Chimie, 2008. 11(8): p. 818-833.
Ogata, H., W. Lubitz, and Y. Higuchi, [NiFe] hydrogenases: structural and spectroscopic studies of the reaction mechanism. Dalton Transactions, 2009(37): p. 7577-7587.
Pereira, A., R. Franco, M. Feio, C. Pinto, J. Lampreia, M. Reis, J. Calvete, I. Moura, I. Beech, and A. Lino, Characterization of representative enzymes from a sulfate reducing bacterium implicated in the corrosion of steel. Biochemical and biophysical research communications, 1996. 221(2): p. 414-421.
Chatelus, C., P. Carrier, P. Saignes, M. Libert, Y. Berlier, P. Lespinat, G. Fauque, and J. Legall, Hydrogenase activity in aged, nonviable Desulfovibrio vulgaris cultures and its significance in anaerobic biocorrosion. Applied and environmental microbiology, 1987. 53(7): p. 1708-1710.
Bryant, R.D. and E.J. Laishley, The role of hydrogenase in anaerobic biocorrosion. Canadian Journal of Microbiology, 1990. 36(4): p. 259-264.
Vignais, P.M. and B. Billoud, Occurrence, classification, and biological function of hydrogenases: an overview. Chemical Reviews, 2007. 107(10): p. 4206-4272.
Adams, M.W. and E.I. Stiefel, Biological hydrogen production: not so elementary. Science, 1998. 282(5395): p. 1842-1843.
Lamle, S.E., S.P. Albracht, and F.A. Armstrong, Electrochemical Potential-Step Investigations of the Aerobic Interconversions of [NiFe]-Hydrogenase from Allochromatium v inosum: Insights into the Puzzling Difference between Unready and Ready Oxidized Inactive States. Journal of the American Chemical Society, 2004. 126(45): p. 14899-14909.
Caffrey, S.M., H.-S. Park, J.K. Voordouw, Z. He, J. Zhou, and G. Voordouw, Function of periplasmic hydrogenases in the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Journal of bacteriology, 2007. 189(17): p. 6159-6167.
Chhabra, S., Q. He, K. Huang, S. Gaucher, E. Alm, Z. He, M. Hadi, T. Hazen, J. Wall, and J. Zhou, Global analysis of heat shock response in Desulfovibrio vulgaris Hildenborough. Journal of bacteriology, 2006. 188(5): p. 1817-1828.
Hantke, K., Iron and metal regulation in bacteria. Current opinion in microbiology, 2001. 4(2): p. 172-177.
Vignais, P.M., B. Billoud, and J. Meyer, Classification and phylogeny of hydrogenases1. FEMS microbiology reviews, 2001. 25(4): p. 455-501.
Fauque, G., H. Peck Jr, J. Moura, B. Huynh, Y. Berlier, D. DerVartanian, M. Teixeira, A. Przybyla, P. Lespinat, and I. Moura, The three classes of hydrogenases from sulfate-reducing bacteria of the genus< i> Desulfovibrio. FEMS microbiology letters, 1988. 54(4): p. 299-344.
Voordouw, G., V. Niviere, F.G. Ferris, P.M. Fedorak, and D.W. Westlake, Distribution of hydrogenase genes in Desulfovibrio spp. and their use in identification of species from the oil field environment. Applied and environmental microbiology, 1990. 56(12): p. 3748-3754.
Rabus, R., T.A. Hansen, and F. Widdel, Dissimilatory sulfate-and sulfur-reducing prokaryotes, in The prokaryotes. 2006, Springer. p. 659-768.
Muyzer, G. and N.B. Ramsing, Molecular methods to study the organization of microbial communities. Water Science and Technology, 1995. 32(8): p. 1-9.
Devereux, R., S. He, C.e.a. Doyle, S. Orkland, D. Stahl, J. LeGall, and W. Whitman, Diversity and origin of Desulfovibrio species: phylogenetic definition of a family. Journal of Bacteriology, 1990. 172(7): p. 3609-3619.
Hansen, T.A., Metabolism of sulfate-reducing prokaryotes. Antonie van Leeuwenhoek, 1994. 66(1-3): p. 165-185.
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