Utilization of hemin and hemoglobin as iron sources by Vibrio parahaemolyticus and identification of an iron-repressible hemin-binding protein

Shigeo Yamamoto, Yoshihiro Hara, Ken ichi Tomochika, Sumino Shinoda

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Several clinical isolates of Vibrio parahaemolyticus were examined for their ability to utilize either hemin or hemoglobin as a sole source of iron. Both compounds appeared to be equally good iron sources. Maximum growth was obtained at 5 μM hemin or 1.25 μM hemoglobin under the conditions tested. Using a hemin-agarose batch affinity method, the hemin-binding protein was isolated from crude total membranes of a hemin-utilizing strain, WP1, grown under iron-deficient but not under iron-sufficient conditions. This protein was identical to the 83 kDa outer membrane protein which was expressed in response to iron limitation. The protein was susceptible to proteinase K cleavage in whole cells, indicating its exposure at the cell surface. Hemin and hemoglobin, but not protoporphyrin IX, inhibited binding of the protein to hemin-agarose.

Original languageEnglish
Pages (from-to)195-200
Number of pages6
JournalFEMS Microbiology Letters
Volume128
Issue number2
DOIs
Publication statusPublished - May 1 1995

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Keywords

  • Hemin utilization
  • Hemin-binding protein
  • Iron source
  • Vibrio parahaemolyticus

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Microbiology
  • Applied Microbiology and Biotechnology

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