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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...

Topics

Bacterial Proteins
Electrophoresis, Gel, Two-Dimensional
Hemoglobins
Mutation
NAD
Oxidation-Reduction
Oxygen

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 1366796
DOI: 10.1038/nbt0990-849

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1366796-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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