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

Saidu Haruna; Hamzat Ibiyeye Tijani; Yusuf Hindatu; Jibrin Ndejiko Mohammed; Bashir Mohammed Abubakar; Mohammed Sulaiman; Abdulrahman Idris

doi:doi:10.11648/j.bio.20140201.11

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

Saidu Haruna, Hamzat Ibiyeye Tijani, Yusuf Hindatu, Jibrin Ndejiko Mohammed, Bashir Mohammed Abubakar, Mohammed Sulaiman, Abdulrahman Idris

Published in American Journal of Bioscience and Bioengineering (Volume 2, Issue 1)

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

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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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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AMA Style

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

Copy | Download

@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}
}

Copy | Download

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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