Hematin iron valence in catalase and peroxidase compound I: relationship to free radical reaction mechanism.
The material in this paper is centered on the structure of compound I (first reaction intermediate) in the case of catalase and a classical peroxidase (horseradish peroxidase, HRP). The concept of a pi-cation radical is accepted for HRP but is rejected in the case of catalase. A possible mechanism for catalatic action previously proposed assumes FeV for the hematin iron of catalase and hydride ion transfer in the reduction of FeV by the second molecule of H2O2, no free radical being involved. In the case of HRP however, FeIV is assumed for compound I. A hypothetical .OH needed to balance the reaction for the formation of compound I is thought to interact with the pi electron cloud of the hematin prosthetic group, forming the now generally accepted pi cation radical and an OH- ion. Attempts to apply the pi cation mechanism to catalatic action lead to contradictions and implausible chemical reactions.
Dounce
A L
AL
Department of Biochemistry and Environmental Health Sciences Center, University of Rochester School of Medicine, NY 14642.
Sichak
S P
SP
D002374:Catalase / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D005609:Free Radicals; D006418:Heme / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism*
D005609:Free Radicals; D006418:Heme; D007501:Iron; D006735:Horseradish Peroxidase; D010544:Peroxidases; D002374:Catalase