Abstract
Ferryl species are important catalytic intermediates in heme enzymes. A recent experimental investigation of a diheme protein MauG reported the first case of using two Fe(IV) species as an alternative to compound I in catalysis. Both Fe(IV) species have unusual Mössbauer properties, which was found to originate from novel structural features based on a quantum chemical investigation. With comparison with the previously reported FeIV=O and FeIV-OH species, results here provide evidence of new mechanisms by which proteins influence the properties of ferryl species by directly providing the O via Tyr or stabilizing exogenous O via hydrogen bonding interaction. These results expand our ability to identify and evaluate high-valent heme proteins and models.
Original language | English |
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Pages (from-to) | 2936-2939 |
Number of pages | 4 |
Journal | Journal of Physical Chemistry Letters |
Volume | 1 |
Issue number | 19 |
DOIs | |
State | Published - 7 Oct 2010 |