Results 31 to 40 of about 42,432 (227)

Turning cellulose waste into electricity: hydrogen conversion by a hydrogenase electrode. [PDF]

open access: yesPLoS ONE, 2013
Hydrogen-producing thermophilic cellulolytic microorganisms were isolated from cow faeces. Rates of cellulose hydrolysis and hydrogen formation were 0.2 mM L(-1) h(-1) and 1 mM L(-1) h(-1), respectively.
Sergey M Abramov   +6 more
doaj   +1 more source

Electron transport phosphorylation in rumen butyrivibrios: unprecedented ATP yield for glucose fermentation to butyrate. [PDF]

open access: yes, 2015
From a genomic analysis of rumen butyrivibrios (Butyrivibrio and Pseudobutyrivibrio sp.), we have re-evaluated the contribution of electron transport phosphorylation (ETP) to ATP formation in this group.
Firkins, Jeffrey L, Hackmann, Timothy J
core   +2 more sources

New insights into [FeFe] hydrogenase activation and maturase function. [PDF]

open access: yesPLoS ONE, 2012
[FeFe] hydrogenases catalyze H(2) production using the H-cluster, an iron-sulfur cofactor that contains carbon monoxide (CO), cyanide (CN(-)), and a dithiolate bridging ligand.
Jon M Kuchenreuther   +2 more
doaj   +1 more source

Synechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditions

open access: yesFrontiers in Microbiology, 2022
The cyanobacterium Synechocystis sp.PCC 6803 possesses a bidirectional NiFe-hydrogenase, HoxEFUYH. It functions to produce hydrogen under dark, fermentative conditions and photoproduces hydrogen when dark-adapted cells are illuminated.
Heinrich Burgstaller   +14 more
doaj   +1 more source

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

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

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

The Geometry of the Catalytic Active Site in [FeFe]-hydrogenases is Determined by Hydrogen Bonding and Proton Transfer [PDF]

open access: yes, 2019
[FeFe]-hydrogenases are efficient metalloenzymes that catalyze the oxidation and evolution of molecular hydrogen, H2. They serve as a blueprint for the design of synthetic H2-forming catalysts.
Apfel, Ulf-Peter   +11 more
core   +2 more sources

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

Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch [PDF]

open access: yes, 2017
[FeFe]-hydrogenases catalyse the reduction of protons to hydrogen at a complex 2Fe[4Fe4S] center called H-cluster. The assembly of this active site is a multistep process involving three proteins, HydE, HydF and HydG.
Acquasaliente, Laura   +8 more
core   +1 more source

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