Nuclear resonance vibrational spectroscopic and computational study of high-valent diiron complexes relevant to enzyme intermediates.

Abstract:

:High-valent intermediates of binuclear nonheme iron enzymes are structurally unknown despite their importance for understanding enzyme reactivity. Nuclear resonance vibrational spectroscopy combined with density functional theory calculations has been applied to structurally well-characterized high-valent mono- and di-oxo bridged binuclear Fe model complexes. Low-frequency vibrational modes of these high-valent diiron complexes involving Fe motion have been observed and assigned. These are independent of Fe oxidation state and show a strong dependence on spin state. It is important to note that they are sensitive to the nature of the Fe2 core bridges and provide the basis for interpreting parallel nuclear resonance vibrational spectroscopy data on the high-valent oxo intermediates in the binuclear nonheme iron enzymes.

authors

Park K,Bell CB 3rd,Liu LV,Wang D,Xue G,Kwak Y,Wong SD,Light KM,Zhao J,Alp EE,Yoda Y,Saito M,Kobayashi Y,Ohta T,Seto M,Que L Jr,Solomon EI

doi

10.1073/pnas.1304238110

subject

Has Abstract

pub_date

2013-04-16 00:00:00

pages

6275-80

issue

16

eissn

0027-8424

issn

1091-6490

pii

1304238110

journal_volume

110

pub_type

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