Disease relevance of Vitreoscilla

• Vitreoscilla cytochrome bo ubiquinol oxidase is similar in some properties to the Escherichia coli enzyme, but unlike the latter, the Vitreoscilla oxidase functions as a primary Na+ pump [1].
• Their functionality as integration vectors has been ascertained by integrating the Vitreoscilla sp. hemoglobin-encoding gene and the Photobacterium leiognathi lux genes [2].
• Application of Vitreoscilla hemoglobin (VHb) technology to 2-CBA degradation by Burkholderia cepacia strain DNT under hypoxic conditions was studied in continuous culture chemostats [3].
• The effects of aldehyde fixation, tannic acid, postfixation, dehydration, temperature, and antigen retrieval on antibody binding activity of Vitreoscilla hemoglobin (VHb) expressed in E. coli cells were assayed by ELISA and the results confirmed by quantitative immunogold labeling transmission electron microscopy (TEM) [4].

High impact information on Vitreoscilla

• Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases [5].
• The binding of cyanide and carbon monoxide to cytochrome o purified from Vitreoscilla. Evidence for subunit interaction in the reduced protein [6].
• The formation of hydrogen peroxide during the oxidation of reduced nicotinamide adenine dinucleotide by cytochrome o from Vitreoscilla [7].
• The first class is typified by the myoglobin-like haemprotein Vgb from the bacterium Vitreoscilla, which has attracted considerable attention because of its ability to improve growth and metabolism for biotechnological gain in a variety of host cells, even though its physiological function is not fully understood [8].
• In the crystalline state, thermodynamics for azide and imidazole binding to ferric Vitreoscilla Hb may be described as a simple process with an overall ligand affinity for the homodimer corresponding to that for diligation in solution [9].

Chemical compound and disease context of Vitreoscilla

• On the other hand, values of the first-order rate constant for cyanide and imidazole dissociation from the diligated and monoligated derivatives of ferric Vitreoscilla Hb in solution are closely similar [9].
• When purified Vitreoscilla cytochrome bo is incorporated into liposomes made from Vitreoscilla phospholipids and energized with a quinol substrate, it translocates Na+, not H+, across the vesicle membrane [1].
• Monomer-dimer equilibrium and oxygen binding properties of ferrous Vitreoscilla hemoglobin [10].
• When ferricytochrome c was entrapped within liposomes prepared from Vitreoscilla phospholipids, it was reduced by Q1H2 (ubiquinol-1) but not by ascorbate/TMPD (N,N,N',N'-tetramethyl-1,4-phenylenediamine) [1].
• Compared to its Hb counterpart from Vitreoscilla strain C1, the purified preparation of V. stercoraria Hb displays a slower autooxidation rate [11].

Biological context of Vitreoscilla

• In sharp contrast to the oxygen-regulated biosynthesis of Hb in Vitreoscilla strain C1, production of Hb in V. stercoraria has been found to be low and independent of oxygen control, which is supported by the absence of a fumarate and nitrate reductase regulator box within the V. stercoraria vgb promoter region [11].
• When these mutants were transformed with a plasmid containing the gene for the bacterial hemoglobin from Vitreoscilla, they were capable of growth in the presence of succinate or lactate and showed aerobic respiration in the presence of these substrates, unlike the parent strains [12].
• Strains of the filamentous gliding bacterium Vitreoscilla, LB13 and C1, are shown to be highly sensitive to UV-A (320-400 nm), with an LD50 of less than 20 kJ m(-2) [13].
• Coexpression of acyl-CoA dehydrogenase gene (yafH) from E. coli and Vitreoscilla hemoglobin gene (vgb) from Vitreoscilla together with the whole A. hydrophila CGMCC 0911 polyhydroxyalkanoate synthesis operon facilitated cell growth and polyhydroxyalkanoate accumulation in E. coli [14].
• Characterization of an inducible oxidative stress response in Vitreoscilla C1 [15].

Anatomical context of Vitreoscilla

• This succinate-supported respiration decreased with successive washings of the vesicles but was restored by adding E. coli cytosol containing the hemoglobin or by adding the hemoglobin purified from Vitreoscilla [12].

Gene context of Vitreoscilla

• The distance between the 3' ends of the Vitreoscilla hemoglobin and uvrA genes is 63 bp [16].
• This very unusual feature can only be accounted for by assuming ligand-linked conformational changes in the monoligated species, which lead to the observed 300-fold decrease in the affinity of cyanide, azide, thiocyanate and imidazole for the monoligated ferric Vitreoscilla Hb with respect to that of the fully unligated homodimer [9].
• Purification, partial characterization, and possible role of catalase in the bacterium Vitreoscilla [17].
• The 24 kDa CyoA soluble domain of Vitreoscilla cytochrome bo quinol oxidase, which pumps out Na(+) during respiration, has been crystallized from a solution of 2 M ammonium sulfate and 5% 2-propanol [18].
• In this study we constructed an artificial flavohemoprotein by fusing Vitreoscilla hemoglobin (VHb) with D-amino acid oxidase (DAO) of Rhodotorula gracilis to determine whether bacterial hemoglobin can be used as an oxygen donor to immobilized flavoenzyme [19].

Analytical, diagnostic and therapeutic context of Vitreoscilla

• Purification, crystallization and preliminary X-ray analysis of the soluble domain of the Na+-pumping cytochrome bo quinol oxidase from Vitreoscilla [18].

References