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Cloning, characterization and expression of the bacterial globin gene from Vitreoscilla in Escherichia coli.
The genomic locus responsible for production of the globin portion of Vitreoscilla hemoglobin (VtHb), the only well-characterized bacterial hemoglobin (Hb), has been cloned and expressed inExpand
Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis
Results suggest that NO metabolizing activity and protection provided by M. smegmatis HbN against toxicity of NO and reactive nitrogen is significantly lower than Hb n of M. tuberculosis. Expand
Role of Pre-A Motif in Nitric Oxide Scavenging by Truncated Hemoglobin, HbN, of Mycobacterium tuberculosis*
Molecular dynamics simulations show that the excision of Pre-A motif results in distinct changes in the protein dynamics, which cause the gate of the tunnel long branch to be trapped into a closed conformation, thus impeding migration of diatomic ligands toward the heme active site. Expand
Oxygen dependent regulation of Vitreoscilla globin gene: evidence for positive regulation by FNR.
Analysis of vgb gene expression and the study on vgb-xylE transcriptional fusion revealed that vgb promoter is preferentially activated in response to oxygen limitation in Vitreoscilla and other heterologous bacterial hosts. Expand
The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases.
Two Escherichia coli mutants that lack both cytochrome o and d terminal oxidases are able to grow with glucose as the carbon source but not with the aerobic substrates succinate or lactate. One ofExpand
Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcriptional fusion.
Results indicate that the vgb gene promoter is transcriptionally regulated by oxygen even in E. coli, and that microaerobiosis is sufficient to induce vgb expression, and also shows that the same promoter is used in both organisms. Expand
Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
It is demonstrated that dimeric haemoglobin, HbN, from M. tuberculosis exhibits distinct nitric oxide dioxygenase (NOD) activity and protects growth and cellular respiration of heterologous hosts, Escherichia coli and Mycobacterium smegmatis, from the toxic effect of exogenous NO and the NO‐releasing compounds. Expand
Mycobacterium tuberculosis Hemoglobin HbO Associates with Membranes and Stimulates Cellular Respiration of RecombinantEscherichia coli * 210
Evidence is provided for the involvement of HbO with the component of aerobic electron transport chain, suggesting that its function may be related to the facilitation of oxygen transfer during aerobic metabolism of M. tuberculosis. Expand
Recent applications of Vitreoscilla hemoglobin technology in bioproduct synthesis and bioremediation
Since its first use in 1990, engineering of heterologous hosts to express the hemoglobin from the bacterium Vitreoscilla has become a widely used strategy to enhance production of a variety of bioproducts, stimulate bioremediation, and increase growth and survival of engineered organisms. Expand
Characteristics of glycosylated streptokinase secreted from Pichia pastoris: enhanced resistance of SK to proteolysis by glycosylation
The results presented illustrate that N-linked glycosylation of SK results in 30–40% enhancement of the protein stability and resistance towards degradation but does not interfere with its fibrinolytic function. Expand