Proton and iodine-127 nuclear magnetic resonance studies on the binding of iodide by lactoperoxidase

Sakurada, Junji; Takahashi, Shunsuke; Shimizu, Tôru; Hatano, Masahiro; Nakamura, Shingo; Hosoya, Toshihiko

doi:10.1021/bi00394a028

Cited by 34 publications

(43 citation statements)

References 30 publications

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“…Because it is very difficult to study the binding to compound I that causes the reaction, the binding of these ions to peroxidases in the resting state was examined by spectrophotometric (4,7,8), kinetic (9,10), fluorometric (11), 127 I NMR (12,13), 15 N NMR (14 -17), 13 C NMR (17), 1 H NMR (13)(14)(15)(16)(17)(18)(19), and optical difference spectroscopy (20 -22) techniques. The actual site of the binding of these ions to the enzymes and the mechanism of electron transfer from these ions to the heme irons have yet to be clarified.…”

mentioning

confidence: 99%

Binding of Iodide to Arthromyces ramosus Peroxidase Investigated with X-ray Crystallographic Analysis, 1H and 127I NMR Spectroscopy, and Steady-state Kinetics

Fukuyama

Sato

Itakura

et al. 1997

Journal of Biological Chemistry

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The site and characteristics of iodide binding to Arthromyces ramosus peroxidase were examined by x-ray crystallographic analysis, 1 H and 127 I NMR, and kinetic studies. X-ray analysis of an A. ramosus peroxidase crystal soaked in a KI solution at pH 5.5 showed that a single iodide ion is located at the entrance of the access channel to the distal side of the heme and lies between the two peptide segments, Phe

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mentioning

confidence: 99%

Binding of Iodide to Arthromyces ramosus Peroxidase Investigated with X-ray Crystallographic Analysis, 1H and 127I NMR Spectroscopy, and Steady-state Kinetics

Fukuyama

Sato

Itakura

et al. 1997

Journal of Biological Chemistry

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“…The K p value of SCN − (24 µM) when compared with the K D value of the enzyme-SCN − complex (15 mM) was found to be significantly lower. The reason for this might be that SCN − binds to the catalytically active enzyme intermediates (ferryl enzyme) with much higher affinity than to the native enzyme, similar to the binding of iodide to HRP [42].…”

Section: Discussionmentioning

confidence: 99%

“…A distal histidine residue in the haem pocket with a pK a value around 6n0 is implicated in the oxidation of various electron donors in peroxidases [43][44][45][46][47][48][49]. Since the observed pK a is a kinetically derived value, its assignment to the histidine group of LGP remains to be established by further experiments.…”

Section: Discussionmentioning

confidence: 99%

Mechanism-based inactivation of lacrimal-gland peroxidase by phenylhydrazine: a suicidal substrate to probe the active site

Mazumdar

Adak

Chatterjee

et al. 1997

Biochemical Journal

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Humans are exposed to various hydrazine derivatives for therapeutic control of several diseases, and mammalian peroxidases are implicated in the oxidative metabolism of many drugs. The results presented here indicate that lacrimal-gland peroxidase is irreversibly inactivated in a mechanism-based way by phenylhydrazine, which acts as a suicidal substrate in the presence of H # O # . The pseudo-first-order kinetic constants for inactivation at pH 5n5 are K i l 18 µM, k inact l 0n25 min −" and τ &! l 2n75 min, with a second-order rate constant of 0n75i10% M −" :min −" . Approx. 27 mol of phenylhydrazine and 54 mol of H # O # are required per mol of enzyme for complete inactivation. The pHdependent inactivation kinetics indicate the involvement of an ionizable group on the enzyme with a pK a value of 5n4, protonation of which favours inactivation. SCN − , the plausible physiological electron donor of the enzyme, protects it from inactivation. Binding studies by optical difference spectroscopy indicate that phenylhydrazine interacts with the enzyme with a K D value of 60 µM, and its binding is prevented by the presence of SCN − . The enzyme is also protected by 5,5-dimethyl-1-pyrroline N-oxide, a free-radical trap, suggesting the involvement of a radical species in the inactivation. ESR studies indicate the formation of a spin-trapped phenyl radical (a N l 15n9 G and

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“…These indicated that ZitB is able to bind both nickel and copper, as well as zinc [316]. NMR signal for iodide binding showed no competition with cyanide and spectra revealed that the binding of iodide is facilitated by protonation of an ionisable group with a pKa value of 6.0-6.8, which was presumed the distal histidyl residue [317].…”

Section: Cadmium ( 111mentioning

confidence: 99%

NMR-Active Nuclei for Biological and Biomedical Applications

Patching¹

2016

J Diagn Imaging Ther

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Nuclear magnetic resonance (NMR) spectroscopy is a principal well-established technique for analysis of chemical, biological, food and environmental samples. This article provides an overview of the properties and applications of NMR-active nuclei (39 nuclei of 33 different elements) used in NMR measurements (solution-and solid-state NMR, magnetic resonance spectroscopy, magnetic resonance imaging) with biological and biomedical systems and samples. The samples include biofluids, cells, tissues, organs or whole body from different organisms (humans, animals, bacteria, fungi, plants) for detecting and quantifying metabolites or environmental samples (water, soils, sediments). Isolated biomolecules (peptides, proteins, nucleic acids) can be analysed for elucidation of atomic-resolution structure, conformation and dynamics and for characterisation of ligand and drug binding, and of protein-ligand, protein-protein and protein-nucleic acid interactions. NMR can be used for drug screening and pharmacokinetics and to provide information in the design and discovery of new drugs. NMR can also measure translocation of ions and small molecules across lipid bilayers and membranes, characterise structure, phase behaviour and dynamics of membranes and elucidate atomic-resolution structure, orientation and dynamics of membrane-embedded peptides and proteins.Keywords: biological and biomedical applications; drug screening; dynamics; magnetic resonance imaging; membrane proteins; metabolomics; MRI; NMR-active nuclei; nuclear magnetic resonance; protein structure INTRODUCTION1 UCLEAR magnetic resonance (NMR) spectroscopy is one of the principal techniques used for analysis of biological and biomedical systems and samples. This can include the identification, quantification and monitoring of ions, small molecules and biomolecules in studies of metabolism and biological function in human and animal cells and tissues, bacterial cells and spores, fungi and plants. Similar types of measurements can be performed on environmental samples such as water, soils and sediment. NMR is able to elucidate atomic-resolution structure, conformation, molecular mechanism, dynamics and exchange processes (on timescales of picoseconds to seconds) in biomolecules, especially peptides, proteins and nucleic acids. NMR can be used for the observation, quantification and characterisation of ligand and drug binding to biomolecules, and for characterisation of ligandprotein, protein-protein and protein-nucleic acid interactions. NMR can be used for drug screening and it can acquire structural, binding and kinetic information for the design and discovery of new drugs. It can then monitor the absorption, distribution, metabolism and excretion (ADME) of administered drugs in pharmacokinetics studies. OPEN ACCESS PEER-REVIEWED*NMR can be used for the observation, quantification and kinetic characterisation of ion and smallmolecule translocation across lipid bilayers and biological membranes, including those of cells, tissues and vesicles. Solid-state NM...

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Proton and iodine-127 nuclear magnetic resonance studies on the binding of iodide by lactoperoxidase

Cited by 34 publications

References 30 publications

Binding of Iodide to Arthromyces ramosus Peroxidase Investigated with X-ray Crystallographic Analysis, 1H and 127I NMR Spectroscopy, and Steady-state Kinetics

Binding of Iodide to Arthromyces ramosus Peroxidase Investigated with X-ray Crystallographic Analysis, 1H and 127I NMR Spectroscopy, and Steady-state Kinetics

Mechanism-based inactivation of lacrimal-gland peroxidase by phenylhydrazine: a suicidal substrate to probe the active site

NMR-Active Nuclei for Biological and Biomedical Applications

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