The Experts below are selected from a list of 405 Experts worldwide ranked by ideXlab platform
Takashi Hayashi - One of the best experts on this subject based on the ideXlab platform.
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supramolecular dimerization of a hexameric hemoprotein via multiple pyrene pyrene interactions
Journal of Porphyrins and Phthalocyanines, 2020Co-Authors: Koji Oohora, Tsuyoshi Mashima, Shota Hirayama, Takashi HayashiAbstract:Protein assemblies are being investigated as a new-class of biomaterials. A supramolecular assembly of a mutant hexameric tyrosine coordinated hemoprotein (HTHP) modified with a pyrene derivative i...
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arginine residues provide a multivalent effect for cellular uptake of a hemoprotein assembly
Chemistry Letters, 2019Co-Authors: Hiroaki Kitagishi, Koji Oohora, Ryota Kajihara, Misa Jiromaru, Takashi HayashiAbstract:Cellular uptake of rigid and flexible supramolecular hemoprotein assemblies formed by cytochrome b562 was investigated. Multivalent cell-penetrating tags on the protein surfaces of the assemblies i...
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a ring shaped hemoprotein trimer thermodynamically controlled by the supramolecular heme heme pocket interaction
Chemical Communications, 2019Co-Authors: Ryota Kajihara, Koji Oohora, Nishiki Fujimaki, Takayuki Uchihashi, Takashi HayashiAbstract:Engineered cytochrome b562, a small hemoprotein, with an externally-attached heme moiety via a moderately long linker at a suitable position predominantly forms a thermodynamically stable ring-shaped trimer in dilute solution. In an equilibrium between supramolecular polymerization and depolymerization, the ring-shaped trimer is kinetically trapped even in a concentrated solution.
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successive energy transfer within multiple photosensitizers assembled in a hexameric hemoprotein scaffold
Physical Chemistry Chemical Physics, 2018Co-Authors: Tsuyoshi Mashima, Koji Oohora, Takashi HayashiAbstract:An assembly of multiple photosensitizers is demonstrated by development of a hexameric hemoprotein (HTHP) scaffold as a light harvesting model to replicate the successive energy transfer occuring within photosensitizer assemblies of natural systems. In our model, six zinc protoporphyrin IX (ZnPP) molecules are arrayed at the heme binding site of HTHP by supramolecular interactions and five fluorescein (Flu) molecules and one Texas Red (Tex) molecule as donor and acceptor photosensitizers, respectively, are attached to the HTHP protein surface with covalent linkages. The flow of excited energy from photoexcited Flu to Tex occurs via two pathways: direct energy transfer from Flu to Tex (path 1) and energy transfer via ZnPP (path 2). Steady state and time-resolved fluorescence measurements reveal that the energy transfer ratio of these pathways (path 1 : path 2) is 39 : 61. These findings indicate that the excited energy originating at five Flu and six ZnPP molecules is collected at one Tex molecule as a funnel-like bottom for light harvesting. The present system using the hexameric hemoprotein scaffold is a promising candidate for construction of an artificial light harvesting system having multiple photosensitizers to promote efficient use of solar energy.
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a supramolecular assembly based on an engineered hemoprotein exhibiting a thermal stimulus driven conversion to a new distinct supramolecular structure
Chemical Communications, 2017Co-Authors: Akira Onoda, Koji Oohora, Yoshitaka Onuma, Yuta Tanaka, Takashi HayashiAbstract:Supramolecular assembly of an engineered hemoprotein with an externally-attached heme moiety via an azobenzene or stilbene linker demonstrates drastic structural transitions between two distinct forms: the thermodynamically stable fiber-type assembly and the kinetically trapped metastable micelle-type assembly induced by transient thermal stimulus.
Koji Oohora - One of the best experts on this subject based on the ideXlab platform.
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supramolecular dimerization of a hexameric hemoprotein via multiple pyrene pyrene interactions
Journal of Porphyrins and Phthalocyanines, 2020Co-Authors: Koji Oohora, Tsuyoshi Mashima, Shota Hirayama, Takashi HayashiAbstract:Protein assemblies are being investigated as a new-class of biomaterials. A supramolecular assembly of a mutant hexameric tyrosine coordinated hemoprotein (HTHP) modified with a pyrene derivative i...
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arginine residues provide a multivalent effect for cellular uptake of a hemoprotein assembly
Chemistry Letters, 2019Co-Authors: Hiroaki Kitagishi, Koji Oohora, Ryota Kajihara, Misa Jiromaru, Takashi HayashiAbstract:Cellular uptake of rigid and flexible supramolecular hemoprotein assemblies formed by cytochrome b562 was investigated. Multivalent cell-penetrating tags on the protein surfaces of the assemblies i...
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a ring shaped hemoprotein trimer thermodynamically controlled by the supramolecular heme heme pocket interaction
Chemical Communications, 2019Co-Authors: Ryota Kajihara, Koji Oohora, Nishiki Fujimaki, Takayuki Uchihashi, Takashi HayashiAbstract:Engineered cytochrome b562, a small hemoprotein, with an externally-attached heme moiety via a moderately long linker at a suitable position predominantly forms a thermodynamically stable ring-shaped trimer in dilute solution. In an equilibrium between supramolecular polymerization and depolymerization, the ring-shaped trimer is kinetically trapped even in a concentrated solution.
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successive energy transfer within multiple photosensitizers assembled in a hexameric hemoprotein scaffold
Physical Chemistry Chemical Physics, 2018Co-Authors: Tsuyoshi Mashima, Koji Oohora, Takashi HayashiAbstract:An assembly of multiple photosensitizers is demonstrated by development of a hexameric hemoprotein (HTHP) scaffold as a light harvesting model to replicate the successive energy transfer occuring within photosensitizer assemblies of natural systems. In our model, six zinc protoporphyrin IX (ZnPP) molecules are arrayed at the heme binding site of HTHP by supramolecular interactions and five fluorescein (Flu) molecules and one Texas Red (Tex) molecule as donor and acceptor photosensitizers, respectively, are attached to the HTHP protein surface with covalent linkages. The flow of excited energy from photoexcited Flu to Tex occurs via two pathways: direct energy transfer from Flu to Tex (path 1) and energy transfer via ZnPP (path 2). Steady state and time-resolved fluorescence measurements reveal that the energy transfer ratio of these pathways (path 1 : path 2) is 39 : 61. These findings indicate that the excited energy originating at five Flu and six ZnPP molecules is collected at one Tex molecule as a funnel-like bottom for light harvesting. The present system using the hexameric hemoprotein scaffold is a promising candidate for construction of an artificial light harvesting system having multiple photosensitizers to promote efficient use of solar energy.
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a supramolecular assembly based on an engineered hemoprotein exhibiting a thermal stimulus driven conversion to a new distinct supramolecular structure
Chemical Communications, 2017Co-Authors: Akira Onoda, Koji Oohora, Yoshitaka Onuma, Yuta Tanaka, Takashi HayashiAbstract:Supramolecular assembly of an engineered hemoprotein with an externally-attached heme moiety via an azobenzene or stilbene linker demonstrates drastic structural transitions between two distinct forms: the thermodynamically stable fiber-type assembly and the kinetically trapped metastable micelle-type assembly induced by transient thermal stimulus.
Mahin D Maines - One of the best experts on this subject based on the ideXlab platform.
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isolation and characterization of a cdna from the rat brain that encodes hemoprotein heme oxygenase 3
FEBS Journal, 1997Co-Authors: William K Mccoubrey, Tian J Huang, Mahin D MainesAbstract:Two isozymes of heme oxygenase (HO), HO-1 or HSP32 and the constitutive form HO-2, have been characterized to date. We report the discovery of a third protein species and refer to it as HO-3. HO-3 is the product of a single transcript of ≈2.4 kb and can encode a protein of ≈33 kDa. The HO-3 transcript is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis and is the product of a single-copy gene. The predicted amino acid structure of HO-3 differs from both HO-1 (HSP32) and HO-2 but is closely related to HO-2 (≈90%). Escherichia coli expressed and purified HO-3 protein does not cross react with polyclonal antibodies to either rat HO-1 or HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics. The predicted protein has two heme regulatory motifs that may be involved in heme binding. These motifs and the hemoprotein nature of HO-3 suggest a potential regulatory role for the protein in cellular processes which are heme-dependent.
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isolation and characterization of a cdna from the rat brain that encodes hemoprotein heme oxygenase 3
FEBS Journal, 1997Co-Authors: William K Mccoubrey, Tian J Huang, Mahin D MainesAbstract:Two isozymes of heme oxygenase (HO), HO-1 or HSP32 and the constitutive form HO-2, have been characterized to date. We report the discovery of a third protein species and refer to it as HO-3. HO-3 is the product of a single transcript of approximately 2.4 kb and can encode a protein of approximately 33 kDa. The HO-3 transcript is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis and is the product of a single-copy gene. The predicted amino acid structure of HO-3 differs from both HO-1 (HSP32) and HO-2 but is closely related to HO-2 (approximately 90%). Escherichia coli expressed and purified HO-3 protein does not cross react with polyclonal antibodies to either rat HO-1 or HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics. The predicted protein has two heme regulatory motifs that may be involved in heme binding. These motifs and the hemoprotein nature of HO-3 suggest a potential regulatory role for the protein in cellular processes which are heme-dependent.
William K Mccoubrey - One of the best experts on this subject based on the ideXlab platform.
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isolation and characterization of a cdna from the rat brain that encodes hemoprotein heme oxygenase 3
FEBS Journal, 1997Co-Authors: William K Mccoubrey, Tian J Huang, Mahin D MainesAbstract:Two isozymes of heme oxygenase (HO), HO-1 or HSP32 and the constitutive form HO-2, have been characterized to date. We report the discovery of a third protein species and refer to it as HO-3. HO-3 is the product of a single transcript of ≈2.4 kb and can encode a protein of ≈33 kDa. The HO-3 transcript is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis and is the product of a single-copy gene. The predicted amino acid structure of HO-3 differs from both HO-1 (HSP32) and HO-2 but is closely related to HO-2 (≈90%). Escherichia coli expressed and purified HO-3 protein does not cross react with polyclonal antibodies to either rat HO-1 or HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics. The predicted protein has two heme regulatory motifs that may be involved in heme binding. These motifs and the hemoprotein nature of HO-3 suggest a potential regulatory role for the protein in cellular processes which are heme-dependent.
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isolation and characterization of a cdna from the rat brain that encodes hemoprotein heme oxygenase 3
FEBS Journal, 1997Co-Authors: William K Mccoubrey, Tian J Huang, Mahin D MainesAbstract:Two isozymes of heme oxygenase (HO), HO-1 or HSP32 and the constitutive form HO-2, have been characterized to date. We report the discovery of a third protein species and refer to it as HO-3. HO-3 is the product of a single transcript of approximately 2.4 kb and can encode a protein of approximately 33 kDa. The HO-3 transcript is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis and is the product of a single-copy gene. The predicted amino acid structure of HO-3 differs from both HO-1 (HSP32) and HO-2 but is closely related to HO-2 (approximately 90%). Escherichia coli expressed and purified HO-3 protein does not cross react with polyclonal antibodies to either rat HO-1 or HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics. The predicted protein has two heme regulatory motifs that may be involved in heme binding. These motifs and the hemoprotein nature of HO-3 suggest a potential regulatory role for the protein in cellular processes which are heme-dependent.
Hiroaki Kitagishi - One of the best experts on this subject based on the ideXlab platform.
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arginine residues provide a multivalent effect for cellular uptake of a hemoprotein assembly
Chemistry Letters, 2019Co-Authors: Hiroaki Kitagishi, Koji Oohora, Ryota Kajihara, Misa Jiromaru, Takashi HayashiAbstract:Cellular uptake of rigid and flexible supramolecular hemoprotein assemblies formed by cytochrome b562 was investigated. Multivalent cell-penetrating tags on the protein surfaces of the assemblies i...
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inside cover self assembly of one and two dimensional hemoprotein systems by polymerization through heme heme pocket interactions angew chem int ed 7 2009
Angewandte Chemie, 2009Co-Authors: Koji Oohora, Hiroaki Kitagishi, Hiroyasu Yamaguchi, Yasuaki Kakikura, Akira Harada, Takashi HayashiAbstract:Supramolecular protein polymers consisting of cytochrome b562 monomers with heme covalently attached to the protein surface are presented by T. Hayashi and co-workers in their Communication on page 1271 ff. Not only one-dimensional hemoprotein fibers with submicrometer lengths have been prepared, but when a heme triad was added as a pivot molecule, two-dimensional protein assembly networks resulted, which cover over 100 square micrometers.
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supramolecular hemoprotein linear assembly by successive interprotein heme heme pocket interactions
Journal of the American Chemical Society, 2007Co-Authors: Hiroaki Kitagishi, Hideaki Sato, Takashi Matsuo, Koji Oohora, Hiroyasu Yamaguchi, And Akira Harada, Takashi HayashiAbstract:We demonstrate a new strategy for the construction of supramolecular hemoprotein assemblies. A synthetic heme was selectively introduced onto the surface Cys residue of the cytochrome b562 single mutant (H63C) through a thioether bond. After removal of the native heme of the H63C mutant by acid denaturation followed by neutralization, the externally attached heme on the apoprotein surface was inserted into the vacant heme pocket of the other apoprotein. Therefore, the interprotein heme−heme pocket interaction produces a unique submicrometer-sized linear hemoprotein fiber, determined by size exclusion chromatography and atomic force microscopy. This methodology should be widely applicable to the creation of new nanobiomaterials based on a functional hemoprotein.