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Nature of O2 and CO binding to metalloporphyrins and heme proteins

Nature of O2 and CO binding to metalloporphyrins and heme proteins

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CO-sensing mechanisms Three toxic gases meet in the mitochondria Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation In vitro heme biotransformation by the HupZ enzyme from Group A streptococcus Mechanism of oxyhaemoglobin breakdown on reaction with acetylphenylhydrazine Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.Quantitative vibrational dynamics of iron in carbonyl porphyrins Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam.13C- and 57Fe-NMR studies of the Fe-C-O unit of heme proteins and synthetic model compounds in solution: comparison with IR vibrational frequencies and X-ray structural data.Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.Small molecule signaling agents: the integrated chemistry and biochemistry of nitrogen oxides, oxides of carbon, dioxygen, hydrogen sulfide, and their derived species Model compounds for the T state of hemoglobin Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding.Carbon monoxide binding to iron porphyrins Solution 1H nuclear magnetic resonance determination of the distal pocket structure of cyanomet complexes of genetically engineered sperm whale myoglobin His64 (E7)-->Val, Thr67 (E10)-->Arg. The role of distal hydrogen bonding by Arg67 (E10) in modu Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin.Iron porphyrins with different imidazole ligands. A theoretical comparative study.Resonance Raman studies of sterically hindered cyanomet "strapped" hemes. Effects of ligand distortion and base tension on iron-carbon bond.Simultaneous observation of the O---O and Fe---O2 stretching modes in oxyhemoglobins On the bonding of FeO2 in hemoglobin and related dioxygen complexes.Resonance Raman investigation of dioxygen bonding in oxycobaltmyoglobin and oxycobalthemoglobin: structural implication of splittings of the bound O--O stretching vibration Heme carbonyls: environmental effects on nu(C-O) and Fe-C/C-O bond length correlations.Structural insights into ligand dynamics: correlated oxygen and picket motion in oxycobalt picket fence porphyrins Influence of NO and (NO)2 adsorption on the properties of Fe-N4 porphyrin-like graphene sheets.Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kinetics Steric control of CO binding in a totally synthetic heme protein model Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue.Modeling heme proteins using atomistic simulations.Iron L-edge X-ray absorption spectroscopy of oxy-picket fence porphyrin: experimental insight into Fe-O2 bonding.Effects of local protein environment on the binding of diatomic molecules to heme in myoglobins. DFT and dispersion-corrected DFT studies.Water may inhibit oxygen binding in hemoprotein models.Identification of carbon-encapsulated iron nanoparticles as active species in non-precious metal oxygen reduction catalysts.NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin.New heme-dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins.Correlated ligand dynamics in oxyiron picket fence porphyrins: structural and Mössbauer investigations.Coupling between oxidation state and hydrogen bond conformation in heme proteins.Kinetics of hemoglobin and transition state theory.Fe-O2 bonding and oxyheme structure in myoglobin CO, NO and O2 as Vibrational Probes of Heme Protein Interactions.Heme isomers substantially affect heme's electronic structure and function.

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

http://www.wikidata.org/entity/Q24561640

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1976 nî lūn-bûn

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1976 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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1976 թվականի հոտեմբերին հրատարակված գիտական հոդված

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1976年の論文

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1976年論文

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1976年論文

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1976年論文

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1976年論文

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1976年論文

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1976年论文

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Proceedings of the National Academy of Sciences of the United States of America

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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J P Collman

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T R Halbert

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P2860

Conformation and cooperativity in hemoglobin.

Ozone model for bonding of an O2 to heme in oxyhemoglobin

Structure of an iron(II) dioxygen complex; a model for oxygen carrying hemeproteins

The carbon monoxide body stores.

Transformation of haemins into bile pigments.

Atmospheric background concentrations of carbon monoxide.

Infrared evidence for similar metal-dioxygen bonding in iron and cobalt oxyhemoglobins.

Properties of hemoglobin A and hemoglobin Zurich (beta63 histidine replaced by arginine): quantitative evaluation of functional abnormalities in hemoglobins.

Moleuclar pathology of human haemoglobin: stereochemical interpretation of abnormal oxygen affinities.

Three-dimensional structure of hemoglobin from the polychaete annelid, Glycera dibranchiata, at 2.5 A resolution.

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10

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73

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John I. Brauman

Kenneth S. Suslick

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1976-10-01T00:00:00Z

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