Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase , while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 220.127.116.11, sulfhydrogenase). Different from EC 18.104.22.168, hydrogen dehydrogenase [NAD(P)+].
four different subunits with the following molecular weights: HndA 18800, HndB 13800, HndC 52000, HndD 63400, SDS-PAGE; four different subunits with the following molecular weights: HndA 19000, HndB 14000, HndC 52000, HndD 64000, SDS-PAGE
the HndC subunit (52 kDa) corresponds to the NADP-reducing unit, and the HndD subunit (63.5 kDa) is homologous to Clostridium pasteurianum hydrogenase. The role of HndA and HndB subunits (18.8 kDa and 13.8 kDa, respectively) in the complex remains unknown. HndAc and HndB can form a heterodimeric intermediate in the electron transfer between the hydrogenase (HndD) active site and the NADP reduction site in HndC
expression in Escherichia coli. The native Escherichia coli maturation machinery will also generate a functional hydrogenase when provided with only the genes encoding the hydrogenase subunits and a single protease from Pyrococcus furiosus. The expression is induced by anaerobic conditions, whereby Escherichia coli is grown aerobically and production of recombinant hydrogenase is achieved by simply changing the gas feed from air to an inert gas (N2). The recombinant enzyme is purified and shown to be functionally similar to the native enzyme purified from Pyrococcus furiosus. The methodology to generate this key hydrogen-producing enzyme has dramatic implications for the production of hydrogen and NADPH as vehicles for energy storage and transport, for engineering hydrogenase to optimize production and catalysis, as well as for the general production of complex, oxygen-sensitive metalloproteins
biohydrogen production. Photochemical hydrogen production system using zinc porphyrin and hydrogenase in a micellar system of cetyltrimethylammonium bromide. Cetyltrimethylammonium bromide acts as a cationic surfactant to effectively separate the charges
biohydrogen production. The enzyme is immobilized between two layers of montmorillonite clay and poly(butylviologen) mixture. The amount of hydrogen produced relates closely to the applied potential, buffer pH and temperature
biohydrogen production from sugars using a mixture of enzymes in an in vitro cell-free synthetic pathway. Development of this process at an industrial scale is limited by the availability of the H2-producing enzyme