Results 131 to 140 of about 112,078 (164)

Physiological and gene expression analysis of inhibition of Desulfovibrio vulgaris hildenborough by nitrite. [PDF]

open access: yesJ Bacteriol, 2004
Haveman SA   +4 more
europepmc   +1 more source

Preemptive biofilm colonization blocks microbial metal corrosion. [PDF]

open access: yesNPJ Biofilms Microbiomes
Ma P, Wang D, Kong W, Xu D, Lovley DR.
europepmc   +1 more source

The adaptive genome of Desulfovibrio vulgaris Hildenborough [PDF]

open access: yesFEMS Microbiology Letters, 2006
Peculiar attributes revealed by sequencing the genome of Desulfovibrio vulgaris Hildenborough are analyzed, particularly in relation to the presence of a phosphotransferase system (PTS). The PTS is a typical bacterial carbohydrate transport system functioning via group translocation.
Margarida Santana
exaly   +4 more sources

The effect of re-oxidation on the reduced hydrogenase of Desulfovibrio vulgaris strain Hildenborough and its oxygen stability [PDF]

open access: yesFEBS Letters, 1983
Upon reduction of the oxygen-stable hydrogenase of Desulfovibrio vulgaris strain Hildenborough this enzyme becomes oxygen sensitive. Only anaerobic oxidation of the reduced enzyme with 2,6-dichlorophenol-indophenol, in the presence of iron and EDTA ...
Dijk, Cees van   +8 more
exaly   +2 more sources

Mutualistic growth of the sulfate-reducer Desulfovibrio vulgaris Hildenborough with different carbohydrates [PDF]

open access: yesMicrobiology, 2012
Desulfovibrio vulgaris Hildenborough genome presents a phosphotransferase system putatively involved in the transport of carbohydrates. However, utilization of sugars by this sulfate-reducing bacterium has never been reported. Herein, we have observed proliferation of D. vulgaris Hildenborough with some carbohydrates, in mutualism with Stenotrophomonas
Maria Carmen Portillo   +2 more
exaly   +4 more sources
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Characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough

2018
The [NiFeSe] hydrogenases are a subgroup of the well-characterized family of [NiFe] hydrogenases, in which a selenocysteine is a ligand to the nickel atom in the binuclear NiFe active site instead of cysteine. These enzymes display very interesting catalytic properties for biological hydrogen production and bioelectrochemical applications: high H2 ...
Sónia, Zacarias   +5 more
openaire   +2 more sources

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