NRVS investigation of ascorbate peroxidase compound II: Observation of Iron(IV)oxo stretching

Ledray, Aaron P.; Mittra, Kaustuv; Green, Michael T.

doi:10.1016/j.jinorgbio.2021.111548

NRVS investigation of ascorbate peroxidase compound II: Observation of Iron(IV)oxo stretching

Journal Article · 01 November 2021 · J. Inorg. Biochem.

DOI:https://doi.org/10.1016/j.jinorgbio.2021.111548· OSTI ID:1820455

Ledray, Aaron P.; Mittra, Kaustuv; Green, Michael T.

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: DOE - Office Of Science; National Institutes of Health (NIH)

OSTI ID:: 1820455

Journal Information:: J. Inorg. Biochem., Vol. 224

Country of Publication:: United States

Language:: ENGLISH

References (32)

Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme Kwon, Hanna; Basran, Jaswir; Casadei, Cecilia M. Nature Communications, Vol. 7, Issue 1 https://doi.org/10.1038/ncomms13445	journal	November 2016
Ascorbate Peroxidase Compound II Is an Iron(IV) Oxo Species Ledray, Aaron P.; Krest, Courtney M.; Yosca, Timothy H. Journal of the American Chemical Society, Vol. 142, Issue 48 https://doi.org/10.1021/jacs.0c09108	journal	November 2020
Selective oxygen transfer catalysed by heme peroxidases: synthetic and mechanistic aspects van Rantwijk, Fred; Sheldon, Roger A. Current Opinion in Biotechnology, Vol. 11, Issue 6 https://doi.org/10.1016/S0958-1669(00)00143-9	journal	December 2000
C-H bond activation in heme proteins: the role of thiolate ligation in cytochrome P450 Green, Michael T. Current Opinion in Chemical Biology, Vol. 13, Issue 1, p. 84-88 https://doi.org/10.1016/j.cbpa.2009.02.028	journal	February 2009
Selective hydroxylation of alkanes by an extracellular fungal peroxygenase: Hydroxylation of alkanes by a fungal peroxygenase Peter, Sebastian; Kinne, Matthias; Wang, Xiaoshi FEBS Journal, Vol. 278, Issue 19 https://doi.org/10.1111/j.1742-4658.2011.08285.x	journal	September 2011
Oxoiron(IV) in Chloroperoxidase Compound II Is Basic: Implications for P450 Chemistry Green, M. T. Science, Vol. 304, Issue 5677 https://doi.org/10.1126/science.1096897	journal	June 2004
Iron(IV)hydroxide pKa and the Role of Thiolate Ligation in C-H Bond Activation by Cytochrome P450 Yosca, T. H.; Rittle, J.; Krest, C. M. Science, Vol. 342, Issue 6160 https://doi.org/10.1126/science.1244373	journal	November 2013
Significantly shorter Fe–S bond in cytochrome P450-I is consistent with greater reactivity relative to chloroperoxidase Krest, Courtney M.; Silakov, Alexey; Rittle, Jonathan Nature Chemistry, Vol. 7, Issue 9 https://doi.org/10.1038/nchem.2306	journal	August 2015
A new look at the role of thiolate ligation in cytochrome P450 Yosca, Timothy H.; Ledray, Aaron P.; Ngo, Joanna JBIC Journal of Biological Inorganic Chemistry, Vol. 22, Issue 2-3 https://doi.org/10.1007/s00775-016-1430-3	journal	January 2017
On the status of ferryl protonation Behan, Rachel K.; Green, Michael T. Journal of Inorganic Biochemistry, Vol. 100, Issue 4 https://doi.org/10.1016/j.jinorgbio.2005.12.019	journal	April 2006
Application of Badger's Rule to Heme and Non-Heme Iron−Oxygen Bonds: An Examination of Ferryl Protonation States Green, Michael T. Journal of the American Chemical Society, Vol. 128, Issue 6 https://doi.org/10.1021/ja054074s	journal	February 2006
The catalytic pathway of horseradish peroxidase at high resolution Berglund, Gunnar I.; Carlsson, Gunilla H.; Smith, Andrew T. Nature, Vol. 417, Issue 6887 https://doi.org/10.1038/417463a	journal	May 2002
An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2 Hersleth, H. -P.; Dalhus, B.; Görbitz, C. JBIC Journal of Biological Inorganic Chemistry, Vol. 7, Issue 3 https://doi.org/10.1007/s007750100296	journal	March 2002
High-Resolution Crystal Structures and Spectroscopy of Native and Compound I Cytochrome c Peroxidase ^† Bonagura, Christopher A.; Bhaskar, B.; Shimizu, Hideaki Biochemistry, Vol. 42, Issue 19 https://doi.org/10.1021/bi034058c	journal	May 2003
Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration. Sitter, A. J.; Reczek, C. M.; Terner, J. Journal of Biological Chemistry, Vol. 260, Issue 12 https://doi.org/10.1016/S0021-9258(17)39637-0	journal	June 1985
Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide p K _a : Insight into Axial Ligand Tuning in Heme Protein Catalysis Yosca, Timothy H.; Behan, Rachel K.; Krest, Courtney M. Journal of the American Chemical Society, Vol. 136, Issue 25 https://doi.org/10.1021/ja503588n	journal	June 2014
Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV) = O bond in compound ES and heme-linked ionization. Hashimoto, S.; Teraoka, J.; Inubushi, T. Journal of Biological Chemistry, Vol. 261, Issue 24 https://doi.org/10.1016/S0021-9258(18)67355-7	journal	August 1986
Resonance Raman characterization of heme Fe(IV)=O groups of intermediates of yeast cytochrome C peroxidase and lactoperoxidase Reczek, Catherine M.; Sitter, Andres J.; Terner, James Journal of Molecular Structure, Vol. 214 https://doi.org/10.1016/0022-2860(89)80004-3	journal	December 1989
Crystallographic and Single-Crystal Spectral Analysis of the Peroxidase Ferryl Intermediate Meharenna, Yergalem T.; Doukov, Tzanko; Li, Huiying Biochemistry, Vol. 49, Issue 14 https://doi.org/10.1021/bi100238r	journal	April 2010
Nuclear resonance vibrational spectroscopy ? NRVS Scheidt, W.; Durbin, S.; Sage, J. Journal of Inorganic Biochemistry, Vol. 99, Issue 1 https://doi.org/10.1016/j.jinorgbio.2004.11.004	journal	January 2005
Nuclear resonant spectroscopy Sturhahn, Wolfgang Journal of Physics: Condensed Matter, Vol. 16, Issue 5 https://doi.org/10.1088/0953-8984/16/5/009	journal	January 2004
Monochromatization of synchrotron radiation for nuclear resonant scattering experiments Toellner, T. S. Hyperfine Interactions, Vol. 125, Issue 1/4, p. 3-28 https://doi.org/10.1023/A:1012621317798	journal	January 2000
Synchrotron-Derived Vibrational Data Confirm Unprotonated Oxo Ligand in Myoglobin Compound II Zeng, Weiqiao; Barabanschikov, Alexander; Zhang, Yunbin Journal of the American Chemical Society, Vol. 130, Issue 6 https://doi.org/10.1021/ja077823+	journal	January 2008
A Combined NRVS and DFT Study of Fe ^IV O Model Complexes: A Diagnostic Method for the Elucidation of Non-Heme Iron Enzyme Intermediates Bell, Caleb B.; Wong, Shaun D.; Xiao, Yuming Angewandte Chemie International Edition, Vol. 47, Issue 47 https://doi.org/10.1002/anie.200803740	journal	November 2008
Probing Hydrogen Bonding Interactions to Iron‐Oxido/Hydroxido Units by ⁵⁷ Fe Nuclear Resonance Vibrational Spectroscopy Weitz, Andrew C.; Hill, Ethan A.; Oswald, Victoria F. Angewandte Chemie International Edition, Vol. 57, Issue 49 https://doi.org/10.1002/anie.201810227	journal	December 2018
What Can Be Learned from Nuclear Resonance Vibrational Spectroscopy: Vibrational Dynamics and Hemes Scheidt, W. Robert; Li, Jianfeng; Sage, J. Timothy Chemical Reviews, Vol. 117, Issue 19 https://doi.org/10.1021/acs.chemrev.7b00295	journal	September 2017
Effects of Noncovalent Interactions on High-Spin Fe(IV)–Oxido Complexes Oswald, Victoria F.; Lee, Justin L.; Biswas, Saborni Journal of the American Chemical Society, Vol. 142, Issue 27 https://doi.org/10.1021/jacs.0c03085	journal	June 2020
Reactivity of an Fe ^IV -Oxo Complex with Protons and Oxidants Hill, Ethan A.; Weitz, Andrew C.; Onderko, Elizabeth Journal of the American Chemical Society, Vol. 138, Issue 40 https://doi.org/10.1021/jacs.6b07633	journal	September 2016
CONUSS and PHOENIX: Evaluation of nuclear resonant scattering data Sturhahn, W. Hyperfine Interactions, Vol. 125, Issue 1/4, p. 149-172 https://doi.org/10.1023/A:1012681503686	journal	March 2000
Resonance Raman spectroscopy of oxoiron(IV) porphyrin π-cation radical and oxoiron(IV) hemes in peroxidase intermediates Terner, James; Palaniappan, Vaithianathan; Gold, Avram Journal of Inorganic Biochemistry, Vol. 100, Issue 4 https://doi.org/10.1016/j.jinorgbio.2006.01.008	journal	April 2006
CO, NO and O2 as vibrational probes of heme protein interactions Spiro, Thomas G.; Soldatova, Alexandra V.; Balakrishnan, Gurusamy Coordination Chemistry Reviews, Vol. 257, Issue 2 https://doi.org/10.1016/j.ccr.2012.05.008	journal	January 2013
CO as a vibrational probe of heme protein active sites Spiro, T.; Wasbotten, I. Journal of Inorganic Biochemistry, Vol. 99, Issue 1 https://doi.org/10.1016/j.jinorgbio.2004.09.026	journal	January 2005

Similar Records

NRVS investigation of ascorbate peroxidase compound II: Observation of Iron(IV)oxo stretching

Journal Article · 2021 · Journal of Inorganic Biochemistry · OSTI ID:1868758

Ledray, Aaron P.; Mittra, Kaustuv; Green, Michael T.

Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration

Journal Article · 1985 · J. Biol. Chem.; (United States) · OSTI ID:6380851

Sitter, A J; Reczek, C M; Terner, J

Vibrational dynamics (IR, Raman, NRVS) and DFT study of new antitumor tetranuclearstannoxanecluster, Sn(IV)$-$oxo$-${di$-$o$-$vanillin} dimethyl dichloride

Journal Article · 2016 · Physical Chemistry Chemical Physics. PCCP (Print) · OSTI ID:1340298

Arjmand, F.; Sharma, S.; Usman, M.; +5 more

NRVS investigation of ascorbate peroxidase compound II: Observation of Iron(IV)oxo stretching

Citation Formats

References (32)

Similar Records

Related Subjects