Results 41 to 50 of about 42,432 (227)

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

Two‐Dimensional Infrared Spectroscopy Reveals the Presence of a Bridging CO Ligand in Two Catalytic Intermediates of [FeFe] Hydrogenase

open access: yesAngewandte Chemie, EarlyView.
Two‐dimensional (2D) infrared (IR) spectroscopy provides vastly more structural and functional insight into chemical and biological systems than linear IR spectroscopy. Here, we apply 2D‐IR spectroscopy to two controversially discussed states of the [FeFe] hydrogenase active site, revealing the presence of a bridging carbonyl ligand, which is difficult
Cornelius C. M. Bernitzky   +7 more
wiley   +2 more sources

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

Recent advances in electron transfer between biofilms and metals [PDF]

open access: yes, 2007
Microbial biofilms produce electrochemical interactions with metal surfaces by following a wide variety of different electron exchange pathways. Reviewing the mechanisms identified in the biocorrosion of steels leads us to distinguish direct and indirect
Bergel, Alain
core   +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

Optimization of carbon and energy utilization through differential translational efficiency. [PDF]

open access: yes, 2018
Control of translation is vital to all species. Here we employ a multi-omics approach to decipher condition-dependent translational regulation in the model acetogen Clostridium ljungdahlii.
Al-Bassam, Mahmoud M   +7 more
core   +2 more sources

Chromatium hydrogenase. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1977
Previous reports of a relatively air-stable soluble hydrogenase from the photosynthetic anaerobe, Chromatium vinosum, have been substantiated. The properties of this enzyme, as seen in highly purified samples prepared by procedures that permit improved yields, are described. A possible role for flavin mediation is noted.
T, Kakuno, N O, Kaplan, M D, Kamen
openaire   +2 more sources

On the pathways feeding the H₂ production process in nutrient-replete, hypoxic conditions : commentary on the article 'Low oxygen levels contribute to improve photohydrogen production in mixotrophic non-stressed Chlamydomonas cultures', by Jurado-Oller et al., Biotechnology for Biofuels, published September 7, 2015; 8:149 [PDF]

open access: yes, 2017
Background: Under low O-2 concentration ( hypoxia) and low light, Chlamydomonas cells can produce H-2 gas in nutrient-replete conditions. This process is hindered by the presence of O-2, which inactivates the [FeFe]-hydrogenase enzyme responsible for H-2
Scoma, Alberto, Toth, Szilvia Z
core   +2 more sources

Diversity and transcription of proteases involved in the maturation of hydrogenases in Nostoc punctiforme ATCC 29133 and Nostoc sp. strain PCC 7120

open access: yesBMC Microbiology, 2009
Background The last step in the maturation process of the large subunit of [NiFe]-hydrogenases is a proteolytic cleavage of the C-terminal by a hydrogenase specific protease.
Lindblad Peter   +3 more
doaj   +1 more source

Making the H-Cluster from Scratch [PDF]

open access: yes, 2014
Spectroscopic data begin to elucidate the initial steps in the biosynthesis of the hydrogenase active site. [Also see Report by Kuchenreuther et al.
Pickett, Christopher
core   +1 more source

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