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Literature summary for 1.14.12.17 extracted from

  • Forrester, M.T.; Eyler, C.E.; Rich, J.N.
    Bacterial flavohemoglobin: a molecular tool to probe mammalian nitric oxide biology (2011), Biotechniques, 50, 41-45.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis heterologous expression of Escherichia coli flavohemoglobin within a lentiviral delivery system boosts endogenous cellular consumption of NO, thus providing a simple and efficacious approach to studying mammalian NO-biology Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
heterologous expression within a lentiviral delivery system Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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General Information

General Information Comment Organism
physiological function heterologous expression within a lentiviral delivery system results in markedly increased NADPH consumption, which is dependent on the addition of exogenous NO. Expression does not exhibit any noticeable toxicity or growth suppression in several tested mammalian cell types. Flavohemoglobin metabolizes endogenously synthesized NO to NO3- in mammalian cells without affecting NO synthesis itself Escherichia coli