% 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},
}