Abstract:
:The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplained. In this study, the reactions of compounds I and II of peroxidase from horseradish with phenols were analyzed using the Marcus equation of electron-transfer. Both reactions exhibit similar reorganization energies, and the different reactivities of the two enzyme states can be ascribed to a higher apparent rate of activationless electron-transfer in the compound I reactions. This can be attributed to the shorter electron-tunneling distance on electron-transfer to the porphyrin radical cation in compound I, compared to electron-transfer to the iron ion in compound II.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Folkes LK,Candeias LPdoi
10.1016/s0014-5793(97)00792-8subject
Has Abstractpub_date
1997-07-28 00:00:00pages
305-8issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00792-8journal_volume
412pub_type
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