Results 21 to 30 of about 17,663 (189)

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

PLoS 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, R David Britt, James R Swartz   +2 more
doaj   +1 more source

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

Frontiers 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, Yingying Wang, Johanna Caliebe, Johanna Caliebe, Vanessa Hueren, Jens Appel, Jens Appel, Marko Boehm, Marko Boehm, Sinje Leitzke, Marius Theune, Marius Theune, Paul W. King, Kirstin Gutekunst, Kirstin Gutekunst   +14 more
doaj   +1 more source

[NiFeSe]-Hydrogenase Chemistry [PDF]

Accounts of Chemical Research, 2015
The development of technology for the inexpensive generation of the renewable energy vector H2 through water splitting is of immediate economic, ecological, and humanitarian interest. Recent interest in hydrogenases has been fueled by their exceptionally high catalytic rates for H2 production at a marginal overpotential, which is presently only matched
Wombwell, Claire, Caputo, Christine A, Reisner, Erwin   +2 more
openaire   +2 more sources

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

PLoS 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, James A Stapleton, James R Swartz   +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

Microorganisms, 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, Sean Craig, Marius Theune, Vanessa Hüren, Sven Künzel, Björn Forberich, Samantha Bryan, Kirstin Gutekunst   +7 more
doaj   +1 more source

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

BMC 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, Manyani Hamid, Imperial Juan, Brito Belén, Ruiz-Argüeso Tomás, Böck August, Palacios Jose-Manuel   +6 more
doaj   +1 more source

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

PLoS 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, Scott Noble, Jonas Korlach, Jin Chen, Carrie Eckert, Jianping Yu, Pin-Ching Maness   +6 more
doaj   +1 more source

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

PLoS 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, Celestine S Grady-Smith, Alyssa S Bingham, Simon J George, Stephen P Cramer, James R Swartz   +5 more
doaj   +1 more source

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

Frontiers 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, Shiny Joseph Srinivasan, Sarah E. Cleary, Peter M. T. Todd, Holly A. Reeve, Kylie A. Vincent   +5 more
doaj   +1 more source

Beyond Canonical CO Oxidation: Structural and Evolutionary Insights Into a Non‐Canonical Carbon Monoxide Dehydrogenase

Angewandte Chemie, EarlyView.
Clade B carbon monoxide dehydrogenases (CODHs) remain enigmatic, diverging from canonical CODHs in structure and function. Here, we present the first characterization of Ruminococcus flavefaciens CODH (RfCODH), revealing occluded substrate pathways and attenuated CO oxidation activity.
Maximilian Böhm, Vivek Srinivas, Benjamin Wiseman, Ping Huang, Moritz Senger, Martin Högbom, Henrik Land   +6 more
wiley   +2 more sources