Molecular hydrogen (H2) is an important molecule in the metabolism of diverse microorganisms. It is used either as energy source or for the disposal of reducing equivalents depending on environmental conditions. Furthermore, H2 transmits energy between different species within microbial communities. The enzymes that split or evolve H2 are called hydrogenases and these metalloproteins can be divided into three phylogenetically unrelated classes distinguishable by the metal composition of their active sites, namely [Fe]-, [FeFe]-, and [NiFe]- hydrogenases. Following a century of hydrogenase research, it is now possible to isolate, handle, and investigate these fragile enzymes. There have been numerous advances in understanding the regulation, function, structures, and maturation of these enzymes, as well as their involvement in important processes such as microbial pathogenesis and biogeochemical cycling. The employment of hydrogenases and hydrogenase-based applications could also potentially facilitate the world’s transition to a future sustainable H2-based energy economy.
Hydrogenases mediate a seemingly simple reaction, i.e. the splitting of H2 into a proton and a hydride, followed by the complete separation of protons and electrons. However, the reaction mechanisms of the different enzyme types are not yet fully understood. Likewise, the complex maturation of the metal cofactors is a constant resource of unprecedented biological chemistry. Additionally, the frequent membrane association and oxygen sensitivity has so far hindered in vitro harnessing of hydrogenase function. New structural data and advances in structure determination may enable new insights into maturation and reaction. In addition, the diverse hydrogenases present in different microorganisms poses questions regarding their physiological functions. Recent attempts to employ hydrogenases for industrial purposes, for example within fuel cells, indicate there is also still a long way to go until biological H2 production will become economically feasible. This Research Topic aims to bring together all recent advances in hydrogenase research, including structure, function, maturation, regulation, and application of hydrogenases to overcome these obstacles. It will also consider environmental, medical, and industrial applications and implications of hydrogenases.
We invite authors to contribute articles that aim at, but are not restricted to, the following themes:
- H2 metabolism in microorganisms
- Analyses of hydrogenase function and regulation
- Structural information of hydrogenases
- Reaction mechanisms of hydrogenases
- Maturation of hydrogenases
- Environmental and medical impact of hydrogenase action
- Biotechnological hydrogenase application in vivo and in vitro
Molecular hydrogen (H2) is an important molecule in the metabolism of diverse microorganisms. It is used either as energy source or for the disposal of reducing equivalents depending on environmental conditions. Furthermore, H2 transmits energy between different species within microbial communities. The enzymes that split or evolve H2 are called hydrogenases and these metalloproteins can be divided into three phylogenetically unrelated classes distinguishable by the metal composition of their active sites, namely [Fe]-, [FeFe]-, and [NiFe]- hydrogenases. Following a century of hydrogenase research, it is now possible to isolate, handle, and investigate these fragile enzymes. There have been numerous advances in understanding the regulation, function, structures, and maturation of these enzymes, as well as their involvement in important processes such as microbial pathogenesis and biogeochemical cycling. The employment of hydrogenases and hydrogenase-based applications could also potentially facilitate the world’s transition to a future sustainable H2-based energy economy.
Hydrogenases mediate a seemingly simple reaction, i.e. the splitting of H2 into a proton and a hydride, followed by the complete separation of protons and electrons. However, the reaction mechanisms of the different enzyme types are not yet fully understood. Likewise, the complex maturation of the metal cofactors is a constant resource of unprecedented biological chemistry. Additionally, the frequent membrane association and oxygen sensitivity has so far hindered in vitro harnessing of hydrogenase function. New structural data and advances in structure determination may enable new insights into maturation and reaction. In addition, the diverse hydrogenases present in different microorganisms poses questions regarding their physiological functions. Recent attempts to employ hydrogenases for industrial purposes, for example within fuel cells, indicate there is also still a long way to go until biological H2 production will become economically feasible. This Research Topic aims to bring together all recent advances in hydrogenase research, including structure, function, maturation, regulation, and application of hydrogenases to overcome these obstacles. It will also consider environmental, medical, and industrial applications and implications of hydrogenases.
We invite authors to contribute articles that aim at, but are not restricted to, the following themes:
- H2 metabolism in microorganisms
- Analyses of hydrogenase function and regulation
- Structural information of hydrogenases
- Reaction mechanisms of hydrogenases
- Maturation of hydrogenases
- Environmental and medical impact of hydrogenase action
- Biotechnological hydrogenase application in vivo and in vitro
