WEKO3
アイテム
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It carries out\u003cbr /\u003evarious functions including the diatomic gaseous ligand storage and transport,electron\u003cbr /\u003etransfer,oxidization,peroxidization,catalysis and signaling process and so on.For \u003cbr /\u003einvestigating the active center, heme-iron-ligand complex,IR and visible RR spectroscopy\u003cbr /\u003ehave revealed the heme environment structure and the ligand discrimination mechanism\u003cbr /\u003efor many heme proteins.Furthermore,electron paramagnetic resonance spectroscopy\u003cbr /\u003eand quantum mechanism study have been used to revealing the reaction mechanism of\u003cbr /\u003eheme enzyme.However, in any cases the accompanying conformational changes in\u003cbr /\u003eprotein moiety always occur for regulating protein function as revealed by x-ray\u003cbr /\u003ecrystallography. It appears quite important to establish a correlation between the active\u003cbr /\u003ecenter, heme,and the protein matrix for understanding the essential mechanism for\u003cbr /\u003eheme proteins. Also,this issue has attracted a lot of concerns from many fields. The\u003cbr /\u003enature utilizes \u003ci\u003eb\u003c/i\u003e type heme as the most common structure among the four kinds of hemes\u003cbr /\u003ethat contain same framework but altered substitutions. Therefore, it is easy to propose\u003cbr /\u003ethat the side chain of heme could play important role in regulation of protein structure\u003cbr /\u003eand function, and this propose is consistent with the discoveries from more and more\u003cbr /\u003eexperimental data that side chains are involved in many reactions related with protein\u003cbr /\u003efunctions. In this study, the interactions between heme and protein matrix as well as solvent leading\u003cbr /\u003eto intramolecular transduction of structural information and intermolecular energy transfer were\u003cbr /\u003esystematically investigated by using Mb. Those interactions include the covalent bond and the\u003cbr /\u003ehydrogen bonds between heme and globin and spatial collision between heme side chains and water\u003cbr /\u003emoleculs.\u003cbr /\u003e In order to investigate the transmission of a binding slgnal of a gaseous ligand from the\u003cbr /\u003eligand binding site?heme,to protein moiety in gas sensory heme proteins,we applied UVRR\u003cbr /\u003espectroscopy to myoglobin as a model. UVRR spectroscopy is known as an excellent tool for\u003cbr /\u003emonitoring protein conformational changes. First of all,we determined the changes of conformation\u003cbr /\u003ein globin that occur upon binding of CO,NO,or O\u003csmall\u003e2\u003c/small\u003eto heme. Specifically,NO induces spectral\u003cbr /\u003e changes in Trp residues of A-helix that are significantly different from those induced by O\u003csmall\u003e2\u003c/small\u003eor CO\u003cbr /\u003ebinding. On the other hand,binding of O\u003csmall\u003e2\u003c/small\u003e to heme produces spectral changes in the Tyr residues of\u003cbr /\u003e H-helix that are difftrent from those induced by CO or NO binding. The UVRR results demonstrate\u003cbr /\u003ethat the heme discriminates among different ligands by driving corresponding conformational changes\u003cbr /\u003e in the globin matrix. In order to explore the signaling pathway through His93 covalent bond,and 6-or\u003cbr /\u003e7-propionate hydrogen bonding network,we extended measurements to mutant-and heme-modified\u003cbr /\u003eMbs in a similar way to native Mb, and investigated how they are responsible for transmitting\u003cbr /\u003estructural changes from ligand binding site--heme to globin for difftrent ligands. The experimental\u003cbr /\u003eresults demonstrate that the cleavage of Fe-His93 covalent bond eliminates communication to the\u003cbr /\u003eC-terminal of the H-helix and that 7-propionate hydrogen-bonding network is essential for\u003cbr /\u003etransmitting the CO or NO binding signal to the N-and C-termini. Finally,6-propionate is important\u003cbr /\u003eonly for NO binding. Thus,the hydrogen-bonding network in the protein appears to be critical for\u003cbr /\u003eintramolecular slgnal transduction in gas sensory heme proteins.\u003cbr /\u003e Furthermore, pathway of vibrational energy dissipation from the heme to\u003cbr /\u003esurrounding protein matrix and solvent following CO photolysis in the fast time\u003cbr /\u003ecomponent (\u0026le;10 ps)was investigated by using picosecond time-resolved anti-Stokes\u003cbr /\u003eRaman spectroscopy. The modified-and mutant Mbs,in which the 6- or 7-propionate is\u003cbr /\u003eselectively replaced by a methyl group or related hydrogen bonds is eliminated by\u003cbr /\u003emutagenesis was used as model systems. The time constants of population decay of\u003cbr /\u003evibrationally excited states for two modified Mbs became significantly larger compared\u003cbr /\u003ewith those of native Mb.However the corresponding values of mutants are not different\u003cbr /\u003efrom those of the native Mb.This work indicates that the two heme-propionate side\u003cbr /\u003echains are highly involved in the energy transfer from the heme to solvent through the\u003cbr /\u003ecollision with surrounding water molecules and contribute equally. But the hydrogen\u003cbr /\u003ebonding interactions with protein matrix seem to contribute scarcely to this fast energy\u003cbr /\u003etransfer process.This is the first experimental data estimating the contribution of\u003cbr /\u003eindividual heme\u003csup\u003e-\u003c/sup\u003epropionate side chains to the vibrational energy transfer from the heme\u003cbr /\u003eto the surroundings.", "subitem_description_type": "Other"}]}, "item_1_description_18": {"attribute_name": "フォーマット", "attribute_value_mlt": [{"subitem_description": "application/pdf", "subitem_description_type": "Other"}]}, "item_1_description_7": {"attribute_name": "学位記番号", "attribute_value_mlt": [{"subitem_description": "総研大甲第1013号", "subitem_description_type": "Other"}]}, "item_1_select_14": {"attribute_name": "所蔵", "attribute_value_mlt": [{"subitem_select_item": "有"}]}, "item_1_select_8": {"attribute_name": "研究科", "attribute_value_mlt": [{"subitem_select_item": "先導科学研究科"}]}, "item_1_select_9": {"attribute_name": "専攻", "attribute_value_mlt": [{"subitem_select_item": "22 光科学専攻"}]}, "item_1_text_10": {"attribute_name": "学位授与年度", "attribute_value_mlt": [{"subitem_text_value": "2006"}]}, "item_creator": {"attribute_name": "著者", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "GAO, Ying", "creatorNameLang": "en"}], "nameIdentifiers": [{"nameIdentifier": "0", "nameIdentifierScheme": "WEKO"}]}]}, "item_files": {"attribute_name": "ファイル情報", "attribute_type": "file", "attribute_value_mlt": [{"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2016-02-17"}], "displaytype": "simple", "download_preview_message": "", "file_order": 0, "filename": "甲1013_要旨.pdf", "filesize": [{"value": "290.8 kB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_11", "mimetype": "application/pdf", "size": 290800.0, "url": {"label": "要旨・審査要旨", "url": "https://ir.soken.ac.jp/record/1249/files/甲1013_要旨.pdf"}, "version_id": "f436ba8d-e6ae-4139-a200-cbb3810228ed"}, {"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2016-02-17"}], "displaytype": "simple", "download_preview_message": "", "file_order": 1, "filename": "甲1013_本文.pdf", "filesize": [{"value": "11.1 MB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_11", "mimetype": "application/pdf", "size": 11100000.0, "url": {"label": "本文", "url": "https://ir.soken.ac.jp/record/1249/files/甲1013_本文.pdf"}, "version_id": "b40349e7-8c2b-4af3-a381-3e42321d5f47"}]}, "item_language": {"attribute_name": "言語", "attribute_value_mlt": [{"subitem_language": "eng"}]}, "item_resource_type": {"attribute_name": "資源タイプ", "attribute_value_mlt": [{"resourcetype": "thesis", "resourceuri": "http://purl.org/coar/resource_type/c_46ec"}]}, "item_title": "Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms", "item_titles": {"attribute_name": "タイトル", "attribute_value_mlt": [{"subitem_title": "Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms"}, {"subitem_title": "Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms", "subitem_title_language": "en"}]}, "item_type_id": "1", "owner": "1", "path": ["24"], "permalink_uri": "https://ir.soken.ac.jp/records/1249", "pubdate": {"attribute_name": "公開日", "attribute_value": "2010-02-22"}, "publish_date": "2010-02-22", "publish_status": "0", "recid": "1249", "relation": {}, "relation_version_is_last": true, "title": ["Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms"], "weko_shared_id": -1}
Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms
https://ir.soken.ac.jp/records/1249
https://ir.soken.ac.jp/records/124948495771-cb8c-4a37-a105-ce3a7ed9f214
名前 / ファイル | ライセンス | アクション |
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Item type | 学位論文 / Thesis or Dissertation(1) | |||||
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公開日 | 2010-02-22 | |||||
タイトル | ||||||
タイトル | Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Resonance Raman Investigation of Protein Dynamics Studies on Myoglobin: Information Transmission and Energy Funneling Mechanisms | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_46ec | |||||
資源タイプ | thesis | |||||
著者名 |
高, 影
× 高, 影 |
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フリガナ |
ガオイン
× ガオイン |
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著者 |
GAO, Ying
× GAO, Ying |
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学位授与機関 | ||||||
学位授与機関名 | 総合研究大学院大学 | |||||
学位名 | ||||||
学位名 | 博士(理学) | |||||
学位記番号 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 総研大甲第1013号 | |||||
研究科 | ||||||
値 | 先導科学研究科 | |||||
専攻 | ||||||
値 | 22 光科学専攻 | |||||
学位授与年月日 | ||||||
学位授与年月日 | 2006-09-29 | |||||
学位授与年度 | ||||||
2006 | ||||||
要旨 | ||||||
内容記述タイプ | Other | |||||
内容記述 | The iron protoporphyrin IX(<i>b</i> type heme)exists as a reaction center in most of the<br />heme proteins as a prosthetic group which bound with the protein matrix. It carries out<br />various functions including the diatomic gaseous ligand storage and transport,electron<br />transfer,oxidization,peroxidization,catalysis and signaling process and so on.For <br />investigating the active center, heme-iron-ligand complex,IR and visible RR spectroscopy<br />have revealed the heme environment structure and the ligand discrimination mechanism<br />for many heme proteins.Furthermore,electron paramagnetic resonance spectroscopy<br />and quantum mechanism study have been used to revealing the reaction mechanism of<br />heme enzyme.However, in any cases the accompanying conformational changes in<br />protein moiety always occur for regulating protein function as revealed by x-ray<br />crystallography. It appears quite important to establish a correlation between the active<br />center, heme,and the protein matrix for understanding the essential mechanism for<br />heme proteins. Also,this issue has attracted a lot of concerns from many fields. The<br />nature utilizes <i>b</i> type heme as the most common structure among the four kinds of hemes<br />that contain same framework but altered substitutions. Therefore, it is easy to propose<br />that the side chain of heme could play important role in regulation of protein structure<br />and function, and this propose is consistent with the discoveries from more and more<br />experimental data that side chains are involved in many reactions related with protein<br />functions. In this study, the interactions between heme and protein matrix as well as solvent leading<br />to intramolecular transduction of structural information and intermolecular energy transfer were<br />systematically investigated by using Mb. Those interactions include the covalent bond and the<br />hydrogen bonds between heme and globin and spatial collision between heme side chains and water<br />moleculs.<br /> In order to investigate the transmission of a binding slgnal of a gaseous ligand from the<br />ligand binding site?heme,to protein moiety in gas sensory heme proteins,we applied UVRR<br />spectroscopy to myoglobin as a model. UVRR spectroscopy is known as an excellent tool for<br />monitoring protein conformational changes. First of all,we determined the changes of conformation<br />in globin that occur upon binding of CO,NO,or O<small>2</small>to heme. Specifically,NO induces spectral<br /> changes in Trp residues of A-helix that are significantly different from those induced by O<small>2</small>or CO<br />binding. On the other hand,binding of O<small>2</small> to heme produces spectral changes in the Tyr residues of<br /> H-helix that are difftrent from those induced by CO or NO binding. The UVRR results demonstrate<br />that the heme discriminates among different ligands by driving corresponding conformational changes<br /> in the globin matrix. In order to explore the signaling pathway through His93 covalent bond,and 6-or<br />7-propionate hydrogen bonding network,we extended measurements to mutant-and heme-modified<br />Mbs in a similar way to native Mb, and investigated how they are responsible for transmitting<br />structural changes from ligand binding site--heme to globin for difftrent ligands. The experimental<br />results demonstrate that the cleavage of Fe-His93 covalent bond eliminates communication to the<br />C-terminal of the H-helix and that 7-propionate hydrogen-bonding network is essential for<br />transmitting the CO or NO binding signal to the N-and C-termini. Finally,6-propionate is important<br />only for NO binding. Thus,the hydrogen-bonding network in the protein appears to be critical for<br />intramolecular slgnal transduction in gas sensory heme proteins.<br /> Furthermore, pathway of vibrational energy dissipation from the heme to<br />surrounding protein matrix and solvent following CO photolysis in the fast time<br />component (≤10 ps)was investigated by using picosecond time-resolved anti-Stokes<br />Raman spectroscopy. The modified-and mutant Mbs,in which the 6- or 7-propionate is<br />selectively replaced by a methyl group or related hydrogen bonds is eliminated by<br />mutagenesis was used as model systems. The time constants of population decay of<br />vibrationally excited states for two modified Mbs became significantly larger compared<br />with those of native Mb.However the corresponding values of mutants are not different<br />from those of the native Mb.This work indicates that the two heme-propionate side<br />chains are highly involved in the energy transfer from the heme to solvent through the<br />collision with surrounding water molecules and contribute equally. But the hydrogen<br />bonding interactions with protein matrix seem to contribute scarcely to this fast energy<br />transfer process.This is the first experimental data estimating the contribution of<br />individual heme<sup>-</sup>propionate side chains to the vibrational energy transfer from the heme<br />to the surroundings. | |||||
所蔵 | ||||||
値 | 有 | |||||
フォーマット | ||||||
内容記述タイプ | Other | |||||
内容記述 | application/pdf |