The Experts below are selected from a list of 5661 Experts worldwide ranked by ideXlab platform
Herbert Witzel - One of the best experts on this subject based on the ideXlab platform.
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evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases 1h nmr studies of the di Iron Derivative of the fe iii zn ii enzyme from kidney bean
Biochemical Journal, 1997Co-Authors: Gianantonio Battistuzzi, Markus Dietrich, Renate Locke, Herbert WitzelAbstract:The di-Iron core of mammalian purple acid phosphatases has been reproduced in the plant enzyme from kidney bean (Mr 111000) upon insertion of an Fe(II) ion in place of the native zinc(II) in the dinuclear Fe(III)Zn(II) core. The shortening of the electronic relaxation time of the metal centre allows detection of hyperfine-shifted 1H NMR resonances, although severe broadening due to Curie relaxation prevents independent signal assignment. Nevertheless, comparison of the spectral features of the structurally characterized plant enzyme with those of the mammalian species, which were previously extensively assigned, is consistent with a close similarity of the metal-binding sites, also suggested by previous sequence-alignment studies. Some differences appear to be mainly localized at the M(II) site. Spectral comparison was also carried out on the Fe(III)Co(II) Derivatives.
Gianantonio Battistuzzi - One of the best experts on this subject based on the ideXlab platform.
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evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases 1h nmr studies of the di Iron Derivative of the fe iii zn ii enzyme from kidney bean
Biochemical Journal, 1997Co-Authors: Gianantonio Battistuzzi, Markus Dietrich, Renate Locke, Herbert WitzelAbstract:The di-Iron core of mammalian purple acid phosphatases has been reproduced in the plant enzyme from kidney bean (Mr 111000) upon insertion of an Fe(II) ion in place of the native zinc(II) in the dinuclear Fe(III)Zn(II) core. The shortening of the electronic relaxation time of the metal centre allows detection of hyperfine-shifted 1H NMR resonances, although severe broadening due to Curie relaxation prevents independent signal assignment. Nevertheless, comparison of the spectral features of the structurally characterized plant enzyme with those of the mammalian species, which were previously extensively assigned, is consistent with a close similarity of the metal-binding sites, also suggested by previous sequence-alignment studies. Some differences appear to be mainly localized at the M(II) site. Spectral comparison was also carried out on the Fe(III)Co(II) Derivatives.
Kevin M. Smith - One of the best experts on this subject based on the ideXlab platform.
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Phenyl Derivative of Iron 5,10,15-Tritolylcorrole
2016Co-Authors: Sara Nardis, Daniel O. Cicero, Silvia Licoccia, Beatrice Berionni Berna, Marco Sette, Giampaolo Ricciardi, Angela Rosa, Frank R. Fronczek, Kevin M. Smith, Roberto PaolesseAbstract:ABSTRACT: The phenyl−Iron complex of 5,10,15-tritolylcorrole was prepared by reaction of the starting chloro−Iron complex with phenylmagnesium bromide in dichloromethane. The organometallic complex was fully characterized by a combination of spectroscopic methods, X-ray crystallography, and density functional theory (DFT) calculations. All of these techniques support the description of the electronic structure of this phenyl−Iron Derivative as a low-spin Iron(IV) coordinated to a closed-shell corrolate trianion and to a phenyl monoanion. Complete assignments of the 1H and 13C NMR spectra of the phenyl−Iron Derivative and the starting chloro−Iron complex were performed on the basis of the NMR spectra of the regioselectively β-substituted bromo Derivatives and the DFT calculations. Corrole was one of the first of the porphyrinoids to be reported in the literature,1 having been prepared during the research wave that focused on the development of a synthetic route t
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Phenyl Derivative of Iron 5,10,15-Tritolylcorrole
2015Co-Authors: Sara Nardis, Daniel O. Cicero, Silvia Licoccia, Giuseppe Pomarico, Beatrice Berionni Berna, Marco Sette, Giampaolo Ricciardi, Angela Rosa, Frank R. Fronczek, Kevin M. SmithAbstract:The phenyl–Iron complex of 5,10,15-tritolylcorrole was prepared by reaction of the starting chloro–Iron complex with phenylmagnesium bromide in dichloromethane. The organometallic complex was fully characterized by a combination of spectroscopic methods, X-ray crystallography, and density functional theory (DFT) calculations. All of these techniques support the description of the electronic structure of this phenyl–Iron Derivative as a low-spin Iron(IV) coordinated to a closed-shell corrolate trianion and to a phenyl monoanion. Complete assignments of the 1H and 13C NMR spectra of the phenyl–Iron Derivative and the starting chloro–Iron complex were performed on the basis of the NMR spectra of the regioselectively β-substituted bromo Derivatives and the DFT calculations
Sara Nardis - One of the best experts on this subject based on the ideXlab platform.
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Phenyl Derivative of Iron 5,10,15-Tritolylcorrole
2016Co-Authors: Sara Nardis, Daniel O. Cicero, Silvia Licoccia, Beatrice Berionni Berna, Marco Sette, Giampaolo Ricciardi, Angela Rosa, Frank R. Fronczek, Kevin M. Smith, Roberto PaolesseAbstract:ABSTRACT: The phenyl−Iron complex of 5,10,15-tritolylcorrole was prepared by reaction of the starting chloro−Iron complex with phenylmagnesium bromide in dichloromethane. The organometallic complex was fully characterized by a combination of spectroscopic methods, X-ray crystallography, and density functional theory (DFT) calculations. All of these techniques support the description of the electronic structure of this phenyl−Iron Derivative as a low-spin Iron(IV) coordinated to a closed-shell corrolate trianion and to a phenyl monoanion. Complete assignments of the 1H and 13C NMR spectra of the phenyl−Iron Derivative and the starting chloro−Iron complex were performed on the basis of the NMR spectra of the regioselectively β-substituted bromo Derivatives and the DFT calculations. Corrole was one of the first of the porphyrinoids to be reported in the literature,1 having been prepared during the research wave that focused on the development of a synthetic route t
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Phenyl Derivative of Iron 5,10,15-Tritolylcorrole
2015Co-Authors: Sara Nardis, Daniel O. Cicero, Silvia Licoccia, Giuseppe Pomarico, Beatrice Berionni Berna, Marco Sette, Giampaolo Ricciardi, Angela Rosa, Frank R. Fronczek, Kevin M. SmithAbstract:The phenyl–Iron complex of 5,10,15-tritolylcorrole was prepared by reaction of the starting chloro–Iron complex with phenylmagnesium bromide in dichloromethane. The organometallic complex was fully characterized by a combination of spectroscopic methods, X-ray crystallography, and density functional theory (DFT) calculations. All of these techniques support the description of the electronic structure of this phenyl–Iron Derivative as a low-spin Iron(IV) coordinated to a closed-shell corrolate trianion and to a phenyl monoanion. Complete assignments of the 1H and 13C NMR spectra of the phenyl–Iron Derivative and the starting chloro–Iron complex were performed on the basis of the NMR spectra of the regioselectively β-substituted bromo Derivatives and the DFT calculations
Markus Dietrich - One of the best experts on this subject based on the ideXlab platform.
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evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases 1h nmr studies of the di Iron Derivative of the fe iii zn ii enzyme from kidney bean
Biochemical Journal, 1997Co-Authors: Gianantonio Battistuzzi, Markus Dietrich, Renate Locke, Herbert WitzelAbstract:The di-Iron core of mammalian purple acid phosphatases has been reproduced in the plant enzyme from kidney bean (Mr 111000) upon insertion of an Fe(II) ion in place of the native zinc(II) in the dinuclear Fe(III)Zn(II) core. The shortening of the electronic relaxation time of the metal centre allows detection of hyperfine-shifted 1H NMR resonances, although severe broadening due to Curie relaxation prevents independent signal assignment. Nevertheless, comparison of the spectral features of the structurally characterized plant enzyme with those of the mammalian species, which were previously extensively assigned, is consistent with a close similarity of the metal-binding sites, also suggested by previous sequence-alignment studies. Some differences appear to be mainly localized at the M(II) site. Spectral comparison was also carried out on the Fe(III)Co(II) Derivatives.
