Abstract
Publisher Summary In aqueous media, without the active methemoglobin reductase system present in intact red blood cells, the ferrous heme groups of hemoglobin can auto-oxidize to form continually increasing amounts of high-spin ferric heme. Under conditions that promote tetramer dissociation, subsequent tertiary structural distortions in the globin monomers occur; these distortions are associated with iron spin-state transitions and possible geometric distortions of the heme moiety within individual heme pockets. Binding of low-spin ferric heme at the sixth coordinate position of the heme iron to normally distant amino acid side chains within the heme pocket can then result in the formation and accumulation of soluble and insoluble hemichromes. This chapter presents a generalized outline of this pathway. An alternate degradative path is also shown, wherein the high-spin ferric heme of hemoglobin is transferred to human serum albumin to form methemalbumin. The apoprotein thus formed is insoluble.
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