Assimilation of metal ions bound to porphyrins or porphyrin-peptides by Vibrio vulnificus, a human pathogen inhabiting estuarine and marine environments

0Citations
Citations of this article
11Readers
Mendeley users who have this article in their library.

Abstract

Vibrio vulnificus, a ubiquitous microorganism in aquatic environments, causes serious septicemia to the immunocompromised host. In addition to protoheme, this species can utilize FeTCPP [ferric tetrakis (4-carboxyphenyl) porphine] as an iron source. In the present study, heme c bound covalently to the protein in cytochrome c, as well as the Fe-TCPP complex formed with a nanopeptide with a high affinity, was found to be useful iron sources for V. vulnificus. This bacterium was also revealed to use Zn-TCPP as a single zinc source. However, other metalloporphyrins such as Mn-TCPP and Pt-TCPP delayed the bacterial growth in the broth containing Fe-TCPP, suggesting interference in the iron assimilation. These results indicate that V. vulnificus may acquire metal ions from both free and peptide-bound metalloporphyrins.

Cite

CITATION STYLE

APA

Miyoshi, S. I., Sasaki, T., Kaku, N., Inoue, T., Uozumi, N., Maehara, Y., & Nakao, H. (2010). Assimilation of metal ions bound to porphyrins or porphyrin-peptides by Vibrio vulnificus, a human pathogen inhabiting estuarine and marine environments. Biocontrol Science, 15(1), 1–6. https://doi.org/10.4265/bio.15.1

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free