% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Moody:860636,
author = {Moody, Peter C. E. and Raven, Emma L.},
title = {{T}he {N}ature and {R}eactivity of {F}erryl {H}eme in
{C}ompounds {I} and {II}},
journal = {Accounts of chemical research},
volume = {51},
number = {2},
issn = {1520-4898},
address = {Columbus, Ohio},
publisher = {American Chemical Soc.},
reportid = {FZJ-2019-01309},
pages = {427 - 435},
year = {2018},
note = {Verantwortlicher für das Instrument: Tobias E. Schrader
JCNS-FRM II},
abstract = {Aerobic organisms have evolved to activate oxygen from the
atmosphere, which allows them to catalyze the oxidation of
different kinds of substrates. This activation of oxygen is
achieved by a metal center (usually iron or copper) buried
within a metalloprotein. In the case of iron-containing heme
enzymes, the activation of oxygen is achieved by formation
of transient iron-oxo (ferryl) intermediates; these
intermediates are called Compound I and Compound II. The
Compound I and II intermediates were first discovered in the
1930s in horseradish peroxidase, and it is now known that
these same species are used across the family of heme
enzymes, which include all of the peroxidases, the heme
catalases, the P450s, cytochrome c oxidase, and NO synthase.
Many years have passed since the first observations, but
establishing the chemical nature of these transient ferryl
species remains a fundamental question that is relevant to
the reactivity, and therefore the usefulness, of these
species in biology.This Account summarizes experiments that
were conceived and conducted at Leicester and presents our
ideas on the chemical nature, stability, and reactivity of
these ferryl heme species. We begin by briefly summarizing
the early milestones in the field, from the 1940s and 1950s.
We present comparisons between the nature and reactivity of
the ferryl species in horseradish peroxidase, cytochrome c
peroxidase, and ascorbate peroxidase; and we consider
different modes of electron delivery to ferryl heme, from
different substrates in different peroxidases.We address the
question of whether the ferryl heme is best formulated as an
(unprotonated) FeIV═O or as a (protonated) FeIV–OH
species. A range of spectroscopic approaches (EXAFS,
resonance Raman, Mossbauer, and EPR) have been used over
many decades to examine this question, and in the last ten
years, X-ray crystallography has also been employed. We
describe how information from all of these studies has
blended together to create an overall picture, and how the
recent application of neutron crystallography has directly
identified protonation states and has helped to clarify the
precise nature of the ferryl heme in cytochrome c peroxidase
and ascorbate peroxidase. We draw comparisons between the
Compound I and Compound II species that we have observed in
peroxidases with those found in other heme systems, notably
the P450s, highlighting possible commonality across these
heme ferryl systems. The identification of proton locations
from neutron structures of these ferryl species opens the
door for understanding the proton translocations that need
to occur during O–O bond cleavage.},
cin = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
ddc = {540},
cid = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106},
pnm = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
Neutron Research (JCNS) (POF3-623)},
pid = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
experiment = {EXP:(DE-MLZ)BIODIFF-20140101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29327921},
UT = {WOS:000426014500024},
doi = {10.1021/acs.accounts.7b00463},
url = {https://juser.fz-juelich.de/record/860636},
}