Abstract
Hydrogen gas is a potential renewable alternative energy carrier that could be used in the future to help supplement humanity's growing energy needs. Unfortunately, current industrial methods for hydrogen production are expensive or environmentally unfriendly. In recent years research has focused on biological mechanisms for hydrogen production and specifically on hydrogenases, the enzyme responsible for catalyzing the reduction of protons to generate hydrogen. In particular, a better understanding of this enzyme might allow us to generate hydrogen that does not use expensive metals, such as platinum, as catalysts. The soluble hydrogenase I (SHI) from the hyperthermophile Pyrococcus furiosus, a member of the euryarchaeota, has been studied extensively and used in various biotechnological applications. This review summarizes the strategies used in engineering and characterizing three different forms of SHI and the properties of the recombinant enzymes. SHI has also been used in in vitro systems for hydrogen production and NADPH generation and these systems are also discussed.
Highlights
Hydrogen is a potential renewable and carbon neutral energy carrier
A major advantage of hydrogen fuel cell vehicles (HFCVs) is that water is the only waste product, and they eliminate the harmful exhaust of current vehicles, thereby benefiting human health and the climate [2, 3]
In order to improve the yield of soluble hydrogenase I (SHI), an attempt was made to heterologously express SHI in E. coli, with coexpression of the genes encoding the accessory proteins that are necessary for proper assembly of the [NiFe] active site [10]
Summary
Hydrogen is a potential renewable and carbon neutral energy carrier. It has three times the energy content per unit mass of fossil fuels [1]. Current methods of producing hydrogen rely on fossil fuels and are expensive They include steam reforming of natural gas, which produces greenhouse gases, and electrolysis to split water uses the expensive metal platinum as a catalyst [4]. The enzyme hydrogenase catalyzes the simplest chemical reaction in nature, the reversible interconversion of protons, electrons, and hydrogen gas: 2H+ + 2e− ↔ H2. Such enzymes are widespread in bacteria and Archaea and are even found in some Eukarya [5]. We focus on the [NiFe] hydrogenases of Pyrococcus furiosus, a strictly anaerobic archaeon that grows optimally at 100∘C This organism utilizes carbohydrates as a carbon source for growth and generates acetate, carbon dioxide, and hydrogen gas as end products. This review focuses on the engineering, properties, and applications of SHI
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