Unprecedented Fe(IV) Species in a Diheme Protein MauG: A Quantum Chemical Investigation on the Unusual Mossbauer Spectroscopic Properties
Chemistry and Biochemistry
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 Mossbauer properties, which was found to originate from novel structural features based on a quantum chemical investigation. With comparison with the previously reported Fe(IV)=O and Fe(IV)-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.
Journal of Physical Chemistry Letters
Davidson, V. L.,
(2010). Unprecedented Fe(IV) Species in a Diheme Protein MauG: A Quantum Chemical Investigation on the Unusual Mossbauer Spectroscopic Properties. Journal of Physical Chemistry Letters, 1(19), 2936-2939.
Available at: http://aquila.usm.edu/fac_pubs/8907