Abstract
Despite extensive work on homolytic versus heterolytic peroxide bond cleavage by iron porphyrins, the nature of the corresponding reactions catalyzed by myoglobin (Mb) and hemoglobin (Hb) remains unclear. These hemoproteins react with peroxides to give a ferryl (Fe IV =O) complex and a protein radical, but the coupling of dioxygen bond cleavage to protein radical formation is obscure. This process is examined here with the help of 4-hydroperoxy-4-methyl-2,6-di-tert-butyl-cyclohexa-2,5-dien-1-one (BHTOOH), a compound that is converted heterolytically to an alcohol and homolytically to several rearranged products
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
