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Catalase‐like activity of bovine met‐hemoglobin: Interaction with the pseudo‐catalytic peroxidation of anthracene traces in aqueous medium
Author(s) -
Paco Laveille,
Galarneau Anne,
Drone Jullien,
Fajula François,
Bailly Carole,
Pulvin Sylviane,
Thomas Daniel
Publication year - 2009
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.200900100
Subject(s) - anthracene , hemoglobin , hydrogen peroxide , chemistry , catalase , peroxidase , catalysis , hemeprotein , myoglobin , photochemistry , stereochemistry , biochemistry , enzyme , heme
Hemoglobin is a member of the hemoprotein superfamily whose main role is to transport O 2 in vertebrate organisms. It has two known promiscuous enzymatic activities, peroxidase and oxygenase. Here we show for the first time that bovine hemoglobin also presents a catalase‐like activity characterized by a V max of 344 μM/min, a K M of 24 mM and a k cat equal to 115/min. For high anthracene and hemoglobin concentrations and low hydrogen peroxide concentrations, this activity inhibits the expected oxidation of anthracene, which occurs through a peroxidase‐like mechanism. Anthracene belongs to the polycyclic aromatic hydrocarbon (PAH) family whose members are carcinogenic and persistent pollutants found in industrial waste waters. Our results show that anthracene oxidation by hemoglobin and hydrogen peroxide follows a typical bi‐bi ping‐pong mechanism with a V max equal to 0.250 μM/min, K M(H2O2) of 80 μM, K M(ANT) of 1.1 μM and k cat of 0.17/min. The oxidation of anthracene is shown to be pseudo‐catalytic because an excess of hemoglobin and hydrogen peroxide is required to make PAH completely disappear. Thus, bovine hemoglobin presents, in different degrees, all the catalytic activities of the hemoprotein group, which makes it a very interesting protein for biotechnological processes and one with which structure‐activity relationships can be studied.