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Utilization of hemin and hemoglobin as iron sources by<i>Vibrio parahaemolyticus</i>and identification of an iron-repressible hemin-binding protein
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Description
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 microM hemin or 1.25 microM 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.
Journal
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- FEMS Microbiology Letters
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FEMS Microbiology Letters 128 195-200, 1995-05-01
Oxford University Press (OUP)
