Results 41 to 50 of about 112,078 (164)
Formic acid (FA) is a promising hydrogen carrier. Formate dehydrogenase catalyzes the CO2 reduction to FA with need of a cofactor that can be regenerated efficiently in a bioelectrochemical system. Bacterial enzyme complexes are capable of dehydrogenating FA to produce hydrogen.
Eleftheria Sapountzaki +3 more
wiley +1 more source
Utilization of Cathodic Hydrogen by Desulfovibrio vulgaris (Hildenborough) [PDF]
Summary: Desulfovibrio vulgaris (Hildenborough) can grow on acetate plus CO2 as carbon source with H2 as the sole source of energy. The capability of sulphate reducers to oxidize H2 has been proposed as a major factor in the anaerobic corrosion of metals. Utilization by D.
I. P. Pankhania +2 more
openaire +1 more source
Genetics and molecular biology of the electron flow for sulfate respiration in Desulfovibrio
Progress in the genetic manipulation of the Desulfovibrio strains has provided an opportunity to explore electron flow pathways during sulfate respiration.
Kimberly L. Keller +4 more
doaj +1 more source
Adaptation via natural selection is an important driver of evolution, and repeatable adaptations of replicate populations, under conditions of a constant environment, have been extensively reported.
Megan L. Kempher +8 more
doaj +1 more source
Simultaneous formate formation from CO2 reduction and cellulose oxidation is enabled by a biohybrid photocatalyst with formate dehydrogenase immobilized on titanium dioxide. The semi‐artificial photocatalytic system can be further immobilized onto floating hollow glass microspheres allowing vertical solar light illumination with optimal light exposure ...
Erwin Lam +5 more
wiley +1 more source
Purification and characterization of the formate dehydrogenase fromDesulfovibrio vulgarisHildenborough [PDF]
Formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, a sulfate-reducing bacterium, has been isolated and characterized. The enzyme is composed of three subunits. A high molecular mass subunit (83,500 Da) is proposed to contain a molybdenum cofactor, a 27,000 Da subunit is found to be similar to the Fe-S subunit of the formate dehydrogenase ...
C, Sebban +3 more
openaire +2 more sources
Rapid genetic and phenotypic adaptation of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough to salt stress was observed during experimental evolution.
Aifen Zhou +19 more
doaj +1 more source
Expanded Diversity of Microbial Groups Capable of Anaerobic Pyrite Reduction and Assimilation of Dissolution Products. [PDF]
Expanded diversity of microbial groups capable of anaerobic pyrite reduction. Devon Payne and Eric Boyd. Different microbial guilds were tested for their ability to reductively dissolve pyrite and mobilize iron and sulfur to support growth. Metabolic guilds capable of pyrite reduction were determined (top) and mechanisms of extracellular electron ...
Boyd ES, Payne D.
europepmc +2 more sources
Tungsten and molybdenum regulation of formate dehydrogenase expression in Desulfovibrio vulgaris Hildenborough. [PDF]
ABSTRACT Formate is an important energy substrate for sulfate-reducing bacteria in natural environments, and both molybdenum- and tungsten-containing formate dehydrogenases have been reported in these organisms. In this work, we studied the effect of both metals on the levels of the three formate dehydrogenases encoded in the ...
da Silva SM +4 more
europepmc +4 more sources
Probing the Structure of [NiFeSe] Hydrogenase with QM/MM Computations
The geometry and vibrational behavior of selenocysteine [NiFeSe] hydrogenase isolated from Desulfovibrio vulgaris Hildenborough have been investigated using a hybrid quantum mechanical (QM)/ molecular mechanical (MM) approach. Structural models have been
Samah Moubarak +3 more
doaj +1 more source

