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Heme binding to albuminoid proteins is the result of recent evolution
Author(s) -
Fasano Mauro,
Fanali Gabriella,
Leboffe Loris,
Ascenzi Paolo
Publication year - 2007
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540701474523
Subject(s) - hemopexin , heme , biochemistry , chemistry , hemeprotein , plasma protein binding , albumin , myoglobin , biology , enzyme
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.iubmb Life, 59: 436‐440, 2007