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The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)

Received: 14 November 2013     Published: 30 December 2013
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Abstract

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.

Published in American Journal of Bioscience and Bioengineering (Volume 2, Issue 1)
DOI 10.11648/j.bio.20140201.11
Page(s) 1-7
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2013. Published by Science Publishing Group

Keywords

Hydrogenases, Sulfate-Reducing Bacteria, Iron-Containing Hydrogenases, Genus: Desulfovibrio, Nickel-Iron-Containing-Hydrogenases, Nickel-Iron-Selenium-Containing Hydrogenases

References
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    Saidu Haruna, Hamzat Ibiyeye Tijani, Yusuf Hindatu, Jibrin Ndejiko Mohammed, Bashir Mohammed Abubakar, et al. (2013). The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp). American Journal of Bioscience and Bioengineering, 2(1), 1-7. https://doi.org/10.11648/j.bio.20140201.11

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    Saidu Haruna; Hamzat Ibiyeye Tijani; Yusuf Hindatu; Jibrin Ndejiko Mohammed; Bashir Mohammed Abubakar, et al. The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp). Am. J. BioSci. Bioeng. 2013, 2(1), 1-7. doi: 10.11648/j.bio.20140201.11

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    Saidu Haruna, Hamzat Ibiyeye Tijani, Yusuf Hindatu, Jibrin Ndejiko Mohammed, Bashir Mohammed Abubakar, et al. The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp). Am J BioSci Bioeng. 2013;2(1):1-7. doi: 10.11648/j.bio.20140201.11

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  • @article{10.11648/j.bio.20140201.11,
      author = {Saidu Haruna and Hamzat Ibiyeye Tijani and Yusuf Hindatu and Jibrin Ndejiko Mohammed and Bashir Mohammed Abubakar and Mohammed Sulaiman and Abdulrahman Idris},
      title = {The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)},
      journal = {American Journal of Bioscience and Bioengineering},
      volume = {2},
      number = {1},
      pages = {1-7},
      doi = {10.11648/j.bio.20140201.11},
      url = {https://doi.org/10.11648/j.bio.20140201.11},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bio.20140201.11},
      abstract = {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.},
     year = {2013}
    }
    

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  • TY  - JOUR
    T1  - The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)
    AU  - Saidu Haruna
    AU  - Hamzat Ibiyeye Tijani
    AU  - Yusuf Hindatu
    AU  - Jibrin Ndejiko Mohammed
    AU  - Bashir Mohammed Abubakar
    AU  - Mohammed Sulaiman
    AU  - Abdulrahman Idris
    Y1  - 2013/12/30
    PY  - 2013
    N1  - https://doi.org/10.11648/j.bio.20140201.11
    DO  - 10.11648/j.bio.20140201.11
    T2  - American Journal of Bioscience and Bioengineering
    JF  - American Journal of Bioscience and Bioengineering
    JO  - American Journal of Bioscience and Bioengineering
    SP  - 1
    EP  - 7
    PB  - Science Publishing Group
    SN  - 2328-5893
    UR  - https://doi.org/10.11648/j.bio.20140201.11
    AB  - 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.
    VL  - 2
    IS  - 1
    ER  - 

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Author Information
  • Department of Biological Sciences, Gombe State University, Gombe, Nigeria

  • Department of Biochemistry, Bauchi State University Gadau, Bauchi, Nigeria

  • Faculty of Bioscience & Medical Engineering, Universiti Teknologi Malaysia, 81310 Skudai, Johor-bahru, Malaysia

  • Department of Microbiology, Ibrahim Badamasi Babangida University Lapai, Niger, Nigeria

  • Department of Biological Sciences, Bauchi State University Gadau, Bauchi, Nigeria

  • Department of Biological Sciences, Gombe State University, Gombe, Nigeria

  • Department of Microbiology, Kaduna State University, Kaduna, Nigeria

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