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


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
Issue number7
Publication statusPublished - 2007


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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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