Наукова періодика України Вісник Львівського університету


Sybirna K. 
Development of the system for heterologous syntesis and maturation of hydrogenases, the most efficient biohydrogen producers / K. Sybirna // Вісник Львівського університету. Серія біологічна. - 2016. - Вип. 73. - С. 123. - Режим доступу: http://nbuv.gov.ua/UJRN/VLNU_biol_2016_73_30
Biohydrogen is considered as an important key to a sustainable power supply and is currently seen as a versatile fuel of the future, with the potential to replace fossil fuels. The most efficient biohydrogen producers are metaloenzymes hydrogenases that reversibly catalyse the reaction: <$Eroman {H sub 2 ~symbol Л~2H sup + ~+~2e sup - }>. Due to inefficient homologous expression, the envisaged strategy for hydrogenase production is the use of a heterologous system, which, however, is hindered by the complex maturation processes of these enzymes. The limit of our understanding in this field makes a barrier for hydrogenasesі application in a variety of biotechnological processes (Sybirna K, Bottin H., 2013). This work focuses on the construction of a new efficient system for heterologous expression and maturation of the [Fe - Fe] hydrogenase from eukaryotic green alga Chlamydomonas reinhardtii (Sybirna K, Antoine T., Lindberg P., et al., 2008) with further enhancement of its catalytic activity (Sybirna K., Ezanno P., Baffert C., et al., 2013). Based on Shewanella oneidensis, which possesses a putative [Fe -Fe] hydrogenase operon, was used as a host for C. reinhardtii [Fe-Fe] hydrogenase production (Sybirna K, Antoine T., Lindberg P., et al., 2008). The purified algal hydrogenase was fully mature and homogeneous in that it bore the predicted full complement of iron. Thus, among the existing systems for heterologous [Fe-Fe] hydrogenase expression and maturation, the one based on S. oneidensis is the most efficient. For C. reinhardtii [Fe - Fe] hydrogenase HydA1 the question of catalytic activity and electron transport is of main importance. It is known that this enzyme directly accepts electrons from ferredoxin which is mediated by some surface residues on hydrogenase. A mutant form of C. reinhardtii hydrogenase was found where aspartic acid in place of arginine 171 leads to a six-fold increase of the catalytic activity in comparison to the wild type protein. At the same time this mutation leads to a strong decrease in ferredoxin-dependent hydrogen production while the catalytic center of mutant forms stays intact (Sybirna K., Ezanno P., Baffert C., et al., 2013). This study highlights the role of electrostatic interactions, via arginine 171, between HydA1 and ferredoxin, the effect of its mutation on electron transfer and, most importantly, the fact that electron transfer to hydrogenase catalytic center is a limiting step in H2 production. The understanding that in the wild-type enzyme H2 production is strongly limited by the electron transfer step will help to create novel enzymes with improved catalytic activity for biotechnological purposes.
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Цитованість авторів публікації:
  • Sybirna K.

  • Бібліографічний опис для цитування:

    Sybirna K. Development of the system for heterologous syntesis and maturation of hydrogenases, the most efficient biohydrogen producers / K. Sybirna // Вісник Львівського університету. Серія біологічна. - 2016. - Вип. 73. - С. 123. - Режим доступу: http://nbuv.gov.ua/UJRN/VLNU_biol_2016_73_30.

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