Publish Your Research Online
Get Recognition - International Audience
Request for an Author Account | Login | Submit Article
|HOME||FAQ||TOP AUTHORS||FORUMS||PUBLISH ARTICLE|
Overview of Hydrogenase EnzymeBY: Sumit Kumar Dubey | Category: Applications | Submitted: 2015-12-24 12:04:25
Article Summary: "Hydrogenase (EC-184.108.40.206) is enzymes that belongs to oxidoreductase family and actively participate in catalysis of reversible reduction of proton to hydrogen molecule. This enzyme possesses keen scope towards the biological hydrogen production..."
Overview of hydrogenase enzyme
Hydrogenase is an active catalyst for the reversible splitting of reduced (H2) to oxidized (H+) form of hydrogen. Proteins such as FNRs (Ferredoxin) and cytochromes can act as physiological electron donors or acceptors for hydrogenase (Vignais et al., 2001). In 1931, Stephenson and Stickland were described hydrogenase. This is the major climb up for research towards efficient biohydrogen production. Biochemical, genetic, spectroscopic, crystallographic and phylogenetic analysis has been applied to understand the structure of hydrogenase. Based on this analysis hydrogenase is classified into three groups: (a). Fe-Fe, (b). Ni-Fe and (c). Fe-only. The Ni-Fe and Fe-Fe hydrogenase both contains an active site and Fe-S (iron-sulfur) cluster. The Fe-only (also known as metal-free hydrogenase) contain only an active site (not Fe-S cluster). Characteristic feature of all hydrogenase is the presence of small CO (Carbon monoxide) molecule and CN-(Cyanide) ions in their active site. This was first detected by FTIR spectroscopic analysis (Song et al., 2007).
Fe-Fe hydrogenase contains Fe-S clusters in their active site. It is the fastest known biological catalysts for hydrogen oxidation and reduction but highly sensitive to oxygen and get inactivated in aerobic environment. Fe-Fe hydrogenase is also reported in few eukaryotes (Vignais and Billoud, 2007).
Two classes of Fe-Fe hydrogenase are recognized:
1. Cytoplasmic, soluble, monomeric, and found in strict anaerobes such as Clostridium pasteurianum (CpI hydrogenase). This is extremely sensitive to inactivation at presence of oxygen. It has been involving in catalysis both hydrogen oxidation and reduction.
2. Periplasmic, heterodimeric, and found in Desulfovibrio sp. It could be purified aerobically, and catalyze mainly Hydrogen oxidation.
Ni-Fe hydrogenase possesses Ni-S and Fe-S clusters. In 2009, the reaction mechanism of Ni-Fe hydrogenase in Desulfovibrio vulgaris was proposed based on X-ray crystallography and spectroscopic data. Results were revealed that during the catalytic process, only the nickel metal ion participates in the redox reaction.
Groups and Sub-groups of Ni-Fe Hydrogenase
Abbreviation: G-Group, SG-Sub group
Fe-only (or hmd hydrogenase) catalyzes the reversible reduction of methenyltetrahydromethanopterin with Hydrogen to methylenetetrahydromethanopterin (Thauer, 1998). This hydrogenase leads the pathway of methane formation from CO2 and H2, and activate only in the presence of a second substrate (methenyl tetrahydromethanopterin). This hydrogenase typically present in methanogenic arechea (Zirngibl et al., 1992).
At present, researchers were focused on improvement of hydrogenases by genetic engineering in order to get the hydrogen production rate up to thauer limit (4.0 mol Hydrogen/ mole of glucose).
1. Ogata, H.; Lubitz, W.; Higuchi, Y. (2009). "[NiFe] hydrogenases: structural and spectroscopic studies of the reaction mechanism". Dalton Trans 37: 7577-7587.
2. Song, L. C., Yang, Z. Y., Hua, Y. J., Wang, H. T., Liu, Y., and Hu, Q. M. 2007. Organometallics, 26, 2106-2110.
3. Thauer, R. K. (1998). Biochemistry of methanogenesis: a tribute to marjory stephenson. 1998 marjory stephenson prize lecture. Microbiology 144(Pt 9), 2377-2406. doi: 10.1099/00221287-144-9-2377
4. Vignais, P.M., Billoud, B. and Meyer, J. (2001). "Classification and phylogeny of hydrogenases". FEMS Microbiol. Rev. 25 (4): 455-501.
5. Vignais, P. M. and Billoud, B. 2007. Occurrence, classification, and biological function of hydrogenases: An overview. Chemical Reviews, 107, 4206-4272.
6. Zirngibl, C., van Dongen, W., Schworer, B., von Biinau, R., Richter, M., Klein, A. & Thauer, R. K. (1992) H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea, Eur. J. Biochem. 208, 511-520.
About Author / Additional Info:
Research Scholar,Department of Biotechnology, NIT Raipur,
Research Interest: Bio-fuels
Comments on this article: (0 comments so far)
• Journey to Bacillus Thuringiensis (BT) Crops
• Giant African Snail - A Pest Now Getting Out of Control
• Adult Stem Cells: Use in Tissue Repairing
• The 23rd Chromosome Disease - Sex Linked Diseases
Latest Articles in "Applications" category:
• Flavor Biotechnology: Part -1
• Flavor Biotechnology: Part -2
• Genetic Engineering Extended the Shelf-life of Fruits
• Biomedical Informatics - From Cells to Populations in the IT Way
• The Concept of Biotechnology: Understanding Various Applications/Uses
• In Vitro Fertilization Procedure - Applications, Advantages and Disadvantages
• Fluorescence-Activated Cell Sorting
• Directed Evolution
• Fermentation, and its Control
• Advanced Fermentation Control Strategies
• Methods of Purification of Enzymes
• Extremophilic Microbes - Organisms Living in Extreme Conditions
• Colorful Bacteria
• Importance of Phytoremediation
• Conservation of Microbes
• Sewage Bacteria - Strictly Anaerobic, Aerobic and Facultative bacteria
• Microbial Growth Substrates
• Injuries to Microbes
• Asepsis and its Importance
Important Disclaimer: All articles on this website are for general information only and is not a professional or experts advice. We do not own any responsibility for correctness or authenticity of the information presented in this article, or any loss or injury resulting from it. We do not endorse these articles, we are neither affiliated with the authors of these articles nor responsible for their content. Please see our disclaimer section for complete terms.
Copyright © 2010 biotecharticles.com - Do not copy articles from this website.
ARTICLE CATEGORIES :
| Disclaimer/Privacy/TOS | Submission Guidelines | Contact Us