Results 31 to 40 of about 35,705 (280)

Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in Escherichia coli

open access: yesMicrobial Cell Factories, 2010
Background Hydrogenases catalyze reversible reaction between hydrogen (H2) and proton. Inactivation of hydrogenase by exposure to oxygen is a critical limitation in biohydrogen production since strict anaerobic conditions are required.
Kim Jaoon YH, Jo Byung, Cha Hyung
doaj   +1 more source

Tyrosine, cysteine, and S-adenosyl methionine stimulate in vitro [FeFe] hydrogenase activation. [PDF]

open access: yesPLoS ONE, 2009
BACKGROUND:[FeFe] hydrogenases are metalloenzymes involved in the anaerobic metabolism of H(2). These proteins are distinguished by an active site cofactor known as the H-cluster.
Jon M Kuchenreuther   +2 more
doaj   +1 more source

Evidence for Electron Transfer from the Bidirectional Hydrogenase to the Photosynthetic Complex I (NDH-1) in the Cyanobacterium Synechocystis sp. PCC 6803

open access: yesMicroorganisms, 2022
The cyanobacterial bidirectional [NiFe]-hydrogenase is a pentameric enzyme. Apart from the small and large hydrogenase subunits (HoxYH) it contains a diaphorase module (HoxEFU) that interacts with NAD(P)+ and ferredoxin. HoxEFU shows strong similarity to
Jens Appel   +7 more
doaj   +1 more source

High-yield expression of heterologous [FeFe] hydrogenases in Escherichia coli. [PDF]

open access: yesPLoS ONE, 2010
BACKGROUND: The realization of hydrogenase-based technologies for renewable H(2) production is presently limited by the need for scalable and high-yielding methods to supply active hydrogenases and their required maturases.
Jon M Kuchenreuther   +5 more
doaj   +1 more source

HydDB: A web tool for hydrogenase classification and analysis

open access: yesScientific Reports, 2016
H2 metabolism is proposed to be the most ancient and diverse mechanism of energy-conservation. The metalloenzymes mediating this metabolism, hydrogenases, are encoded by over 60 microbial phyla and are present in all major ecosystems.
Dan Søndergaard   +2 more
semanticscholar   +1 more source

Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum

open access: yesBMC Microbiology, 2012
Background [NiFe] hydrogenases are enzymes that catalyze the oxidation of hydrogen into protons and electrons, to use H2 as energy source, or the production of hydrogen through proton reduction, as an escape valve for the excess of reduction equivalents ...
Albareda Marta   +6 more
doaj   +1 more source

Genome annotation provides insight into carbon monoxide and hydrogen metabolism in Rubrivivax gelatinosus. [PDF]

open access: yesPLoS ONE, 2014
We report here the sequencing and analysis of the genome of the purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS. This microbe is a model for studies of its carboxydotrophic life style under anaerobic condition, based on its ability ...
Karen Wawrousek   +6 more
doaj   +1 more source

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

open access: yesChemical Reviews, 2016
Hydrogenase enzymes efficiently process H2 and protons at organometallic FeFe, NiFe, or Fe active sites. Synthetic modeling of the many H2ase states has provided insight into H2ase structure and mechanism, as well as afforded catalysts for the H2 energy ...
D. Schilter   +4 more
semanticscholar   +1 more source

Integration of a Hydrogenase in a Lead Halide Perovskite Photoelectrode for Tandem Solar Water Splitting

open access: yesACS Energy Letters, 2019
Lead halide perovskite solar cells are notoriously moisture-sensitive, but recent encapsulation strategies have demonstrated their potential application as photoelectrodes in aqueous solution. However, perovskite photoelectrodes rely on precious metal co-
Esther Edwardes Moore   +4 more
semanticscholar   +1 more source

H2-Driven Reduction of Flavin by Hydrogenase Enables Cleaner Operation of Nitroreductases for Nitro-Group to Amine Reductions

open access: yesFrontiers in Catalysis, 2022
Hydrogenase-mediated reduction of flavin mononucleotide by H2 is exploited to enable cleaner application of nitroreductase enzymes for reduction of aromatic nitro functional groups. This turns the overall reaction into a biocatalytic hydrogenation.
Miguel A. Ramirez   +5 more
doaj   +1 more source

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