Heme binding to albuminoid proteins is the result of recent evolution

Mauro Fasano, Gabriella Fanali, Loris Leboffe, Paolo Ascenzi

Research output: Contribution to journalArticlepeer-review

Abstract

We hypothesize that the structure of the heme binding site of paralogous albuminoids alpha-fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered albuminoid. Heme binding to plasma proteins should serve not only as a buffer for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.

Original languageEnglish
Pages (from-to)436-440
Number of pages5
JournalIUBMB Life
Volume59
Issue number7
DOIs
Publication statusPublished - 2007

Keywords

  • Comparative modeling
  • Docking simulation
  • Hemoproteins
  • Molecular evolution
  • Protein structure

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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