FeFehydrogenases

FeFe hydrogenases are a class of enzymes that catalyze the reversible reduction of protons (H+) to molecular hydrogen (H2) or the oxidation of molecular hydrogen to protons. They are named for their active site, which contains a [FeFe] cluster consisting of two iron atoms bridged by two sulfur atoms. This cluster is responsible for the enzyme's ability to transfer electrons and protons.

FeFe hydrogenases are found in a variety of organisms, including bacteria, archaea, and some eukaryotes. They play a crucial role in the metabolism of these organisms, facilitating the production or consumption of hydrogen gas. In some cases, FeFe hydrogenases are involved in the detoxification of hydrogen peroxide, a byproduct of oxygen metabolism.

The structure of FeFe hydrogenases is highly conserved, with a common fold consisting of an N-terminal domain, a [FeFe] hydrogenase domain, and a C-terminal domain. The N-terminal domain is involved in substrate binding and activation, while the C-terminal domain is involved in electron transfer. The [FeFe] hydrogenase domain contains the active site and is responsible for the catalytic activity of the enzyme.

FeFe hydrogenases are of significant interest in biotechnology due to their ability to catalyze the production of hydrogen gas. They are being studied as potential catalysts for hydrogen production from renewable energy sources, such as water splitting. Additionally, FeFe hydrogenases are being investigated for their potential use in bioremediation, as they can catalyze the reduction of toxic compounds, such as heavy metals and halogenated hydrocarbons.

Despite their potential applications, the mechanism of FeFe hydrogenases is not fully understood. Ongoing research aims to elucidate the structural and functional aspects of these enzymes, with the ultimate goal of developing more efficient and stable hydrogenase catalysts.