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Article

Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli.

Bio/technology (Nature Publishing Company) - 1 Sept 1990

Khosla C, Curtis J E, DeModena J, Rinas U, Bailey J E

Abstract excerpt

We have previously cloned the Vitreoscilla hemoglobin gene (VHb) and expressed the protein in Escherichia coli in its active form. Under oxygen-limited conditions the presence of VHb improves protein synthesis as indicated by both total protein content and the activity of an enzyme expressed from a cloned gene present on a multicopy plasmid. Measurements of nitrogen utilization rates corroborate the observation...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 1366796
DOI: 10.1038/nbt0990-849

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli.PMID 1366796Read ↗

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A mutation that improves soluble recombinant hemoglobin accumulation in Escherichia coli in heme excess.Semantic proximity Read ↗

Error-prone PCR of Vitreoscilla hemoglobin (VHb) to support the growth of microaerobic Escherichia coli.Semantic proximity Read ↗

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Selection and characterization of alpha-amylase-overproducing recombinant Escherichia coli containing the bacterial hemoglobin gene.Semantic proximity Read ↗

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