Open AccessUtilization of hemin and hemoglobin as iron sources by Vibrio parahaemolyticus and identification of an iron‐repressible hemin‐binding protein
Author(s) -
Yamamoto Shigeo,
Hara Yoshihiro,
Tomochika Kenichi,
Shinoda Sumino
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07522.x
Subject(s) - hemin , vibrio parahaemolyticus , hemoglobin , biochemistry , agarose , chemistry , heme , protoporphyrin , biology , microbiology and biotechnology , chromatography , bacteria , enzyme , porphyrin , genetics
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.