Crystallographic and Single-Crystal Spectral Analysis of the Peroxidase Ferryl Intermediate
- 15 March 2010
- journal article
- other
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 49 (14), 2984-2986
- https://doi.org/10.1021/bi100238r
Abstract
The ferryl [Fe(IV)O] intermediate is important in many heme enzymes, and thus, the precise nature of the Fe(IV)−O bond is critical in understanding enzymatic mechanisms. The 1.40 Å crystal structure of cytochrome c peroxidase Compound I has been determined as a function of X-ray dose while the visible spectrum was being monitored. The Fe−O bond increases in length from 1.73 Å in the low-X-ray dose structure to 1.90 Å in the high-dose structure. The low-dose structure correlates well with an Fe(IV)═O bond, while we postulate that the high-dose structure is the cryo-trapped Fe(III)−OH species previously thought to be an Fe(IV)−OH species.Keywords
This publication has 14 references indexed in Scilit:
- Absorbed dose calculations for macromolecular crystals: improvements to RADDOSEJournal of Synchrotron Radiation, 2009
- The Influence of X‐Rays on the Structural Studies of Peroxide‐Derived Myoglobin IntermediatesChemistry & Biodiversity, 2008
- Engineering Ascorbate Peroxidase Activity into Cytochrome c PeroxidaseBiochemistry, 2008
- On the status of ferryl protonationJournal of Inorganic Biochemistry, 2006
- Application of Badger's Rule to Heme and Non-Heme Iron−Oxygen Bonds: An Examination of Ferryl Protonation StatesJournal of the American Chemical Society, 2006
- Oxoiron(IV) in Chloroperoxidase Compound II Is Basic: Implications for P450 ChemistryScience, 2004
- High-Resolution Crystal Structures and Spectroscopy of Native and Compound I Cytochrome c PeroxidaseBiochemistry, 2003
- The catalytic pathway of horseradish peroxidase at high resolutionNature, 2002
- An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2JBIC Journal of Biological Inorganic Chemistry, 2002
- Identification by ENDOR of Trp 191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ESScience, 1989