Page last updated: 2024-08-23

heme and ferryl iron

heme has been researched along with ferryl iron in 26 studies

Research

Studies (26)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (7.69)18.2507
2000's11 (42.31)29.6817
2010's11 (42.31)24.3611
2020's2 (7.69)2.80

Authors

AuthorsStudies
Minetti, M; Pietraforte, D; Scorza, G1
Adelroth, P; Brzezinski, P; Gennis, RB; Smirnova, IA; Zaslavsky, D1
Chouchane, S; Lippai, I; Magliozzo, RS1
Costas, M; Kaizer, J; Que, L1
Hlavica, P1
Decker, A; Solomon, EI1
Que, L; Rohde, JU1
Echalier, A; Pauleta, SR; Pettigrew, GW1
Alayash, AI; Buehler, PW; Caron, A; Cooper, CE; Dunne, J; Faivre, B; Menu, P; Silaghi-Dumitrescu, R; Wilson, MT1
Davydov, R; Dawson, JH; Hoffman, BM; Kim, SH; Osborne, RL1
Bell, CB; Cramer, SP; Klinker, EJ; Que, L; Rohde, JU; Smith, MC; Solomon, EI; Tenderholt, AL; Wong, SD; Xiao, Y1
Cho, J; Dhuri, SN; Fukuzumi, S; Kubo, M; Lee, YM; Nam, W; Ogura, T; Sawant, SC1
Abeykoon, A; Krishnan, S; Rusling, JF; Schenkman, JB1
Gennis, RB; Konstantinov, AA; Siletsky, SA; Zhu, J1
Gumiero, A; Metcalfe, CL; Moody, PC; Pearson, AR; Raven, EL1
Bischin, C; Cooper, CE; Damian, G; Deac, F; Rajagopal, BS; Silaghi-Dumitrescu, R; Worrall, JA1
Alayash, AI; Buehler, PW; Bulow, L; Cooper, CE; Reeder, BJ; Schaer, DJ; Silkstone, G; Svistunenko, DA; Wilson, MT1
Garcia-Bosch, I; Karlin, KD; Sharma, SK1
Fukuzumi, S; Lee, YM; Nam, W1
Boaz, NC; Groves, JT1
Basran, J; Blakeley, MP; Casadei, CM; Concilio, MG; Fielding, AJ; Gumiero, A; Metcalfe, CL; Moody, PC; Murphy, EJ; Ostermann, A; Raven, EL; Schrader, TE; Teixeira, SC1
Liu, H; Liu, Q; Zhang, X; Zhou, X; Zhou, Z1
Alayash, AI; Jana, S; Jia, Y; Kassa, T; Meng, F; Strader, MB; Wilson, MT1
de Visser, SP; Li, XX; Luis, JM; Postils, V; Saint-André, M; Solà, M; Timmins, A; Wang, Y1
de Visser, SP; Green, AP; Lee, CWZ; Mubarak, MQE1
Bagha, UK; Barman, P; de Visser, SP; Kumar, D; Mukherjee, G; Sastri, CV; Satpathy, JK1

Reviews

2 review(s) available for heme and ferryl iron

ArticleYear
Models and mechanisms of O-O bond activation by cytochrome P450. A critical assessment of the potential role of multiple active intermediates in oxidative catalysis.
    European journal of biochemistry, 2004, Volume: 271, Issue:22

    Topics: Animals; Catalysis; Cytochrome P-450 Enzyme System; Ferric Compounds; Heme; Hemin; Humans; Hydroxylation; Iron; Models, Molecular; Oxidation-Reduction; Oxygen; Thermodynamics

2004
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
    Journal of inorganic biochemistry, 2006, Volume: 100, Issue:4

    Topics: Amino Acid Sequence; Bacterial Proteins; Crystallography, X-Ray; Cytochrome-c Peroxidase; Electron Transport; Enzyme Activation; Heme; Iron; Models, Biological; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Conformation; Structure-Activity Relationship

2006

Other Studies

24 other study(ies) available for heme and ferryl iron

ArticleYear
Peroxynitrite induces long-lived tyrosyl radical(s) in oxyhemoglobin of red blood cells through a reaction involving CO2 and a ferryl species.
    Biochemistry, 1999, Feb-16, Volume: 38, Issue:7

    Topics: Carbon Dioxide; Electron Spin Resonance Spectroscopy; Erythrocytes; Ferric Compounds; Free Radicals; Heme; Hemoglobins; Humans; Hydrogen Peroxide; Iron; Methemoglobin; Metmyoglobin; Nitrates; Oxidants; Oxygen; Oxyhemoglobins; Tyrosine

1999
Observation of a novel transient ferryl complex with reduced CuB in cytochrome c oxidase.
    Biochemistry, 1999, Feb-23, Volume: 38, Issue:8

    Topics: Animals; Cattle; Copper; Electron Transport; Electron Transport Complex IV; Heme; Hydrogen Peroxide; Iron; Kinetics; Oxidation-Reduction; Oxygen; Protons

1999
Catalase-peroxidase (Mycobacterium tuberculosis KatG) catalysis and isoniazid activation.
    Biochemistry, 2000, Aug-15, Volume: 39, Issue:32

    Topics: Bacterial Proteins; Dimerization; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Iron; Isoniazid; Mycobacterium tuberculosis; Peroxidases; Recombinant Proteins; Spectrum Analysis, Raman

2000
A dramatic push effect on the homolysis of FeIII(OOR) intermediates to form non-heme FeIV=O complexes.
    Angewandte Chemie (International ed. in English), 2003, Aug-11, Volume: 42, Issue:31

    Topics: Ferric Compounds; Heme; Iron; Molecular Structure; Oxidation-Reduction; Pyridines

2003
Comparison of FeIV=O heme and non-heme species: electronic structures, bonding, and reactivities.
    Angewandte Chemie (International ed. in English), 2005, Apr-08, Volume: 44, Issue:15

    Topics: Electrons; Heme; Hydrogen Bonding; Iron; Macromolecular Substances; Models, Chemical; Molecular Structure; Nonheme Iron Proteins; Oxygen

2005
Axial coordination of carboxylate activates the non-heme FeIV=O unit.
    Angewandte Chemie (International ed. in English), 2005, Apr-08, Volume: 44, Issue:15

    Topics: Carboxylic Acids; Heme; Iron; Ligands; Molecular Structure; Nonheme Iron Proteins; Organometallic Compounds; Oxygen; Tetraethylammonium Compounds; Trifluoroacetic Acid

2005
Ascorbate removes key precursors to oxidative damage by cell-free haemoglobin in vitro and in vivo.
    The Biochemical journal, 2006, Nov-01, Volume: 399, Issue:3

    Topics: Animals; Ascorbic Acid; Blood Substitutes; Cell-Free System; Electron Spin Resonance Spectroscopy; Erythrocyte Membrane; Erythrocytes; Exchange Transfusion, Whole Blood; Free Radicals; Heme; Hemodilution; Hemoglobin A; Humans; Hydrogen Peroxide; Iron; Male; Methemoglobin; Methemoglobinemia; Oxidation-Reduction; Oxidative Stress; Oxyhemoglobins; Peroxides; Rabbits; Transferrin

2006
EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl hemes.
    Biochemistry, 2008, May-06, Volume: 47, Issue:18

    Topics: Animals; Armoracia; Electron Spin Resonance Spectroscopy; Electrons; Heme; Horses; Humans; Iron; Kinetics; Myoglobin; Oxidation-Reduction; Peroxidases; Protons

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.
    Angewandte Chemie (International ed. in English), 2008, Volume: 47, Issue:47

    Topics: Enzymes; Fourier Analysis; Heme; Iron; Models, Chemical; Nonheme Iron Proteins; Nuclear Magnetic Resonance, Biomolecular; Vibration

2008
Water as an oxygen source in the generation of mononuclear nonheme iron(IV) oxo complexes.
    Angewandte Chemie (International ed. in English), 2009, Volume: 48, Issue:10

    Topics: Catalysis; Cerium; Heme; Iron; Oxidation-Reduction; Oxygen; Spectrophotometry, Ultraviolet; Water

2009
Control of electrochemical and ferryloxy formation kinetics of cyt P450s in polyion films by heme iron spin state and secondary structure.
    Journal of the American Chemical Society, 2009, Nov-11, Volume: 131, Issue:44

    Topics: Cytochrome P-450 Enzyme System; Electrochemical Techniques; Electron Transport; Heme; Humans; Iron; Kinetics; Molecular Structure; Protein Structure, Secondary

2009
Partial steps of charge translocation in the nonpumping N139L mutant of Rhodobacter sphaeroides cytochrome c oxidase with a blocked D-channel.
    Biochemistry, 2010, Apr-13, Volume: 49, Issue:14

    Topics: Amino Acid Substitution; Electricity; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Iron; Liposomes; Membrane Potentials; Oxidation-Reduction; Oxygen; Photochemical Processes; Rhodobacter sphaeroides

2010
Nature of the ferryl heme in compounds I and II.
    The Journal of biological chemistry, 2011, Jan-14, Volume: 286, Issue:2

    Topics: Ascorbate Peroxidases; Crystallography, X-Ray; Cytochrome-c Peroxidase; Heme; Hemoglobins; Iron; Myoglobin; Oxyhemoglobins; Peroxidases; Protein Structure, Tertiary; Protons; Stereoisomerism

2011
Ascorbate peroxidase activity of cytochrome c.
    Free radical research, 2011, Volume: 45, Issue:4

    Topics: Animals; Apoptosis; Ascorbic Acid; Cardiolipins; Cattle; Cytochrome-c Peroxidase; Cytochromes c; Free Radicals; Guanidine; Heme; Horses; Hydrogen Peroxide; Iron; Kinetics; Methylation; Mitochondria, Heart; Signal Transduction; Spectrum Analysis; Yeasts

2011
Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145.
    Antioxidants & redox signaling, 2013, Jun-10, Volume: 18, Issue:17

    Topics: Electron Spin Resonance Spectroscopy; Free Radicals; Haptoglobins; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Iron; Lipid Peroxidation; Oxidation-Reduction; Protein Binding; Protein Stability; Tyrosine

2013
A selective stepwise heme oxygenase model system: an iron(IV)-oxo porphyrin π-cation radical leads to a verdoheme-type compound via an isoporphyrin intermediate.
    Journal of the American Chemical Society, 2013, Nov-06, Volume: 135, Issue:44

    Topics: Cations; Free Radicals; Heme; Heme Oxygenase (Decyclizing); Iron; Metalloporphyrins; Molecular Structure

2013
Tuning reactivity and mechanism in oxidation reactions by mononuclear nonheme iron(IV)-oxo complexes.
    Accounts of chemical research, 2014, Apr-15, Volume: 47, Issue:4

    Topics: Biomimetics; Electrons; Heme; Iron; Ligands; Oxidation-Reduction; Oxygen; Protons; Water

2014
Biochemistry. Fishing for peroxidase protons.
    Science (New York, N.Y.), 2014, Jul-11, Volume: 345, Issue:6193

    Topics: Cytochrome-c Peroxidase; Heme; Iron

2014
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.
    Science (New York, N.Y.), 2014, Jul-11, Volume: 345, Issue:6193

    Topics: Crystallography, X-Ray; Cytochrome-c Peroxidase; Heme; Histidine; Iron; Neutron Diffraction; Neutrons; Oxygen; Protons

2014
Fractional transfer of a free unpaired electron to overcome energy barriers in the formation of Fe(4+) from Fe(3+) during the core contraction of macrocycles: implication for heme distortion.
    Organic & biomolecular chemistry, 2015, Mar-14, Volume: 13, Issue:10

    Topics: Catalysis; Cobalt; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Electrons; Free Radicals; Heme; Ions; Iron; Models, Molecular; Molecular Conformation; Molecular Structure; Oxidation-Reduction; Oxygen; Porphyrins

2015
Sickle Cell Hemoglobin in the Ferryl State Promotes βCys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10).
    The Journal of biological chemistry, 2015, Nov-13, Volume: 290, Issue:46

    Topics: Anemia, Hemolytic; Anemia, Sickle Cell; Catalysis; Cyclic N-Oxides; Cysteine; Energy Metabolism; Heme; Heme Oxygenase (Decyclizing); Hemoglobin, Sickle; Humans; Hydrogen Peroxide; Iron; Lung; Methemoglobin; Mitochondria; Oxidation-Reduction; Oxygen Consumption; Respiratory Mucosa

2015
Quantum Mechanics/Molecular Mechanics Studies on the Relative Reactivities of Compound I and II in Cytochrome P450 Enzymes.
    International journal of molecular sciences, 2018, Jul-06, Volume: 19, Issue:7

    Topics: Catalysis; Catalytic Domain; Cytochrome P-450 Enzyme System; Electron Transport; Heme; Humans; Hydrogen; Iron; Molecular Conformation; Molecular Dynamics Simulation; Oxidants; Oxygen; Quantum Theory

2018
How Does Replacement of the Axial Histidine Ligand in Cytochrome
    International journal of molecular sciences, 2020, Sep-27, Volume: 21, Issue:19

    Topics: Catalysis; Catalytic Domain; Computational Biology; Cytochrome-c Peroxidase; Ferric Compounds; Heme; Horseradish Peroxidase; Hydrogen Bonding; Hydrogen Peroxide; Iron; Ligands; Methylhistidines; Oxidation-Reduction; Protein Engineering

2020
Oxidative dehalogenation of halophenols by high-valent nonheme iron(IV)-oxo intermediates.
    Faraday discussions, 2022, 05-18, Volume: 234, Issue:0

    Topics: Heme; Iron; Oxidation-Reduction; Oxidative Stress

2022