Unprecedented Fe(IV) species in a diheme protein MauG: A quantum chemical investigation on the unusual Mössbauer spectroscopic properties

Yan Ling, Victor L. Davidson, Yong Zhang

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

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 languageEnglish
Pages (from-to)2936-2939
Number of pages4
JournalJournal of Physical Chemistry Letters
Volume1
Issue number19
DOIs
StatePublished - 7 Oct 2010

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