AI Article Synopsis
- The [NiFeSe] hydrogenases are a unique subgroup of hydrogenases, characterized by the presence of selenocysteine as a ligand to nickel in their active site.
- These enzymes exhibit notable catalytic properties, making them promising for biological hydrogen production and bioelectrochemical uses, including high hydrogen production, preference for hydrogen evolution, low inhibition from hydrogen, and partial tolerance to oxygen.
- The text discusses the methods used to study the [NiFeSe] hydrogenase from D. vulgaris Hildenborough and the development of a system to produce variant forms of this enzyme.
Article Abstract
The [NiFeSe] hydrogenases are a subgroup of the well-characterized family of [NiFe] hydrogenases, in which a selenocysteine is a ligand to the nickel atom in the binuclear NiFe active site instead of cysteine. These enzymes display very interesting catalytic properties for biological hydrogen production and bioelectrochemical applications: high H production activity, bias for H evolution, low H inhibition, and some degree of O tolerance. Here we describe the methodologies employed to study the [NiFeSe] hydrogenase isolated from the sulfate-reducing bacteria D. vulgaris Hildenborough and the creation of a homologous expression system for production of variant forms of the enzyme.
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| http://dx.doi.org/10.1016/bs.mie.2018.10.003 | DOI Listing |
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