| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M701948200 |
| P698 | PubMed publication ID | 17565988 |
| P50 | author | Hans-Petter Hersleth | Q49747797 |
| Takeshi Uchida | Q61093964 | ||
| Åsmund K Røhr | Q61446992 | ||
| P2093 | author name string | Carl Henrik Görbitz | |
| K Kristoffer Andersson | |||
| Teizo Kitagawa | |||
| Alfred X Trautwein | |||
| Volker Schünemann | |||
| Thomas Teschner | |||
| P2860 | cites work | Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination | Q26778405 |
| Processing of X-ray diffraction data collected in oscillation mode | Q26778468 | ||
| Crystal structures of myoglobin-ligand complexes at near-atomic resolution | Q27619924 | ||
| An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2 | Q27638748 | ||
| The catalytic pathway of horseradish peroxidase at high resolution | Q27639029 | ||
| High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase | Q27641217 | ||
| Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography | Q27643492 | ||
| Laue diffraction study on the structure of cytochrome c peroxidase compound I | Q27730880 | ||
| Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy | Q27733832 | ||
| Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide | Q27766717 | ||
| Use of TLS parameters to model anisotropic displacements in macromolecular refinement | Q27860499 | ||
| Coot: model-building tools for molecular graphics | Q27860505 | ||
| Automated refinement of protein models | Q27860928 | ||
| The CCP4 suite: programs for protein crystallography | Q27861090 | ||
| Expanding the model: anisotropic displacement parameters in protein structure refinement. | Q30322708 | ||
| When X-rays modify the protein structure: radiation damage at work. | Q30350508 | ||
| The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement. | Q30955561 | ||
| Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction | Q31029767 | ||
| Emerging roles for myoglobin in the heart | Q33186685 | ||
| Heme-Containing Oxygenases | Q34114428 | ||
| X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry | Q34133320 | ||
| Redox reactions of hemoglobin and myoglobin: biological and toxicological implications | Q34276285 | ||
| The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology | Q34368813 | ||
| The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin | Q34459642 | ||
| A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure. | Q34480651 | ||
| High-valent transition metal centers versus noninnocent ligands in metallocorroles: insights from electrochemistry and implications for high-valent heme protein intermediates | Q34784206 | ||
| Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide | Q35033663 | ||
| Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mössbauer properties | Q35053354 | ||
| Intermediates in P450 catalysis | Q36131575 | ||
| Structural biology of heme monooxygenases | Q36268555 | ||
| On the status of ferryl protonation | Q36406266 | ||
| Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases. | Q36410677 | ||
| High-valent nonheme iron-oxo species in biomimetic oxidations | Q36418827 | ||
| Crystallization and preliminary diffraction data for horse heart metmyoglobin | Q36466728 | ||
| Transport of oxygen in muscle | Q38624113 | ||
| Mössbauer spectroscopy on nonequilibrium states of myoglobin: a study of r-t relaxation | Q39662316 | ||
| Protein dynamics in an intermediate state of myoglobin: optical absorption, resonance Raman spectroscopy, and x-ray structure analysis | Q40162154 | ||
| Evidence for basic ferryls in cytochromes P450. | Q40238639 | ||
| Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance | Q40787431 | ||
| Structural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase | Q41710656 | ||
| pH-dependent forms of the ferryl haem in myoglobin peroxide analysed by variable-temperature magnetic circular dichroism | Q42836620 | ||
| The reaction between metmyoglobin and hydrogen peroxide | Q42951895 | ||
| Metal- and ligand-centered monoelectronic oxidation of mu-nitrido[((tetraphenylporphyrinato)manganese)phthalocyaninatoiron)], [(TPP)Mn-N-FePc]. X-ray crystal structure of the Fe(IV)-containing species [(THF)(TPP)Mn-N-FePc(H(2)O)](I(5))02THF. | Q43634776 | ||
| Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin | Q43687037 | ||
| Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin | Q43842616 | ||
| Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy | Q43918096 | ||
| The nature of the high-valent complexes in the catalytic cycles of hemoproteins | Q44857478 | ||
| Role of myoglobin in the antioxidant defense of the heart | Q44888055 | ||
| Probing the free radicals formed in the metmyoglobin-hydrogen peroxide reaction | Q44889984 | ||
| Resonance Raman spectroscopy of oxoiron(IV) porphyrin pi-cation radical and oxoiron(IV) hemes in peroxidase intermediates | Q44917774 | ||
| Structural and functional diversity in heme monooxygenases | Q45099280 | ||
| Transient intermediates in the reduction of Fe(III) myoglobin-ligand complexes by electrons at low temperature | Q45810683 | ||
| Ferrylmyoglobin: formation and chemical reactivity toward electron-donating compounds. | Q45989386 | ||
| Toward identification of the compound I reactive intermediate in cytochrome P450 chemistry: a QM/MM study of its EPR and Mössbauer parameters | Q46444997 | ||
| Rapid freeze-quench 57Fe Mössbauer spectroscopy: monitoring changes of an iron-containing active site during a biochemical reaction | Q46461921 | ||
| High-valent nonheme iron. Two distinct iron(IV) species derived from a common iron(II) precursor | Q46619817 | ||
| Mechanisms of reoxygenation injury in myocardial infarction: implications of a myoglobin redox cycle | Q46713623 | ||
| Electronic ménages a trois: a molecular orbital perspective of protonated ferryl intermediates and synthetic models | Q46965573 | ||
| Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry | Q47358710 | ||
| The structure of heme proteins Compounds I and II: some misconceptions | Q47975052 | ||
| Evidence for two ferryl species in chloroperoxidase compound II. | Q50731788 | ||
| Application of Badger's rule to heme and non-heme iron-oxygen bonds: an examination of ferryl protonation states. | Q50740231 | ||
| A multiple wavelength analysis of the reaction between hydrogen peroxide and metmyoglobin. | Q52887761 | ||
| Demonstration of peroxodiferric intermediate in M-ferritin ferroxidase reaction using rapid freeze-quench Mössbauer, resonance Raman, and XAS spectroscopies. | Q53663150 | ||
| Defining Redox State of X-Ray Crystal Structures by Single-Crystal Ultraviolet–Visible Microspectrophotometry | Q56836501 | ||
| Crystallographic and Spectroscopic Characterization of a Nonheme Fe(IV)&cjs0811;O Complex | Q56863614 | ||
| The structures ofMicrococcus lysodeikticuscatalase, its ferryl intermediate (compound II) and NADPH complex | Q56896362 | ||
| Structures of Nonheme Oxoiron(IV) Complexes from X-ray Crystallography, NMR Spectroscopy, and DFT Calculations | Q57250564 | ||
| Conformational Analysis of Mitochondrial and Microsomal Cytochrome P-450 by Resonance Raman Spectroscopy | Q57654286 | ||
| Resonance Raman Spectroscopic Studies of Hydroperoxo-Myoglobin at Cryogenic Temperatures | Q58035730 | ||
| Formation and Decay of Hydroperoxo-Ferric Heme Complex in Horseradish Peroxidase Studied by Cryoradiolysis | Q58035737 | ||
| Nitric oxide moves myoglobin centre stage | Q58070399 | ||
| Two-State Reactivity, Electromerism, Tautomerism, and “Surprise” Isomers in the Formation of Compound II of the Enzyme Horseradish Peroxidase from the Principal Species, Compound I | Q58095147 | ||
| Reaction of Methæmoglobin with Hydrogen Peroxide | Q59047358 | ||
| P433 | issue | 32 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 23372-86 | |
| P577 | publication date | 2007-08-10 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O | |
| P478 | volume | 282 |
| Q27695583 | Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model |
| Q30402180 | Correlated single-crystal electronic absorption spectroscopy and X-ray crystallography at NSLS beamline X26-C. |
| Q58035694 | Cryoradiolysis as a Method for Mechanistic Studies in Inorganic Biochemistry |
| Q38683342 | Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature. |
| Q43159966 | Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study |
| Q57163909 | Dynamics in the heme geometry of myoglobin induced by the one-electron reduction |
| Q30413166 | Dynamics-stability relationships in apo- and holomyoglobin: a combined neutron scattering and molecular dynamics simulations study |
| Q42154931 | Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediates |
| Q82435435 | High-valent diiron species generated from N-bridged diiron phthalocyanine and H2O2 |
| Q30392420 | How different oxidation states of crystalline myoglobin are influenced by X-rays |
| Q30574665 | Internal water and microsecond dynamics in myoglobin |
| Q36184084 | Introducing DInaMo: A Package for Calculating Protein Circular Dichroism Using Classical Electromagnetic Theory |
| Q84629329 | Mechanistic insight from thermal activation parameters for oxygenation reactions of different substrates with biomimetic iron porphyrin models for compounds I and II |
| Q27305203 | Molecular dynamic simulations reveal the structural determinants of Fatty Acid binding to oxy-myoglobin |
| Q45092518 | Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin |
| Q36373683 | Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction |
| Q48044973 | Reactivity Patterns of (Protonated) Compound II and Compound I of Cytochrome P450: Which is the Better Oxidant? |
| Q24599611 | Review: studies of ferric heme proteins with highly anisotropic/highly axial low spin (S = 1/2) electron paramagnetic resonance signals with bis-histidine and histidine-methionine axial iron coordination |
| Q33879188 | Setting an upper limit on the myoglobin iron(IV)hydroxide pK(a): insight into axial ligand tuning in heme protein catalysis |
| Q35896446 | Slow histidine H/D exchange protocol for thermodynamic analysis of protein folding and stability using mass spectrometry |
| Q46881369 | Stereospinomers of pentacoordinate iron porphyrin complexes: the case of the [Fe(porphyrinato)(CN)]- anions |
| Q54473080 | The McClure and Weiss models of Fe-O2 bonding for oxyhemes, and the HbO2 + NO reaction. |
| Q27678500 | The reductive reaction mechanism of tobacco nitrite reductase derived from a combination of crystal structures and ultraviolet-visible microspectroscopy |
| Q35590292 | Tryptophan-to-heme electron transfer in ferrous myoglobins |
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