{"_buckets": {"deposit": "39f841f6-a7c9-4660-8480-5034380107a3"}, "_deposit": {"created_by": 1, "id": "1249", "owners": [1], "pid": {"revision_id": 0, "type": "depid", "value": "1249"}, "status": "published"}, "_oai": {"id": "oai:ir.soken.ac.jp:00001249", "sets": ["24"]}, "author_link": ["0", "0", "0"], "item_1_biblio_info_21": {"attribute_name": "書誌情報（ソート用）", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2006-09-29", "bibliographicIssueDateType": "Issued"}, "bibliographic_titles": [{}]}]}, "item_1_creator_2": {"attribute_name": "著者名", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "高, 影"}], "nameIdentifiers": [{"nameIdentifier": "0", "nameIdentifierScheme": "WEKO"}]}]}, "item_1_creator_3": {"attribute_name": "フリガナ", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "ガオイン"}], "nameIdentifiers": [{"nameIdentifier": "0", "nameIdentifierScheme": "WEKO"}]}]}, "item_1_date_granted_11": {"attribute_name": "学位授与年月日", "attribute_value_mlt": [{"subitem_dategranted": "2006-09-29"}]}, "item_1_degree_grantor_5": {"attribute_name": "学位授与機関", "attribute_value_mlt": [{"subitem_degreegrantor": [{"subitem_degreegrantor_name": "総合研究大学院大学"}]}]}, "item_1_degree_name_6": {"attribute_name": "学位名", "attribute_value_mlt": [{"subitem_degreename": "博士（理学）"}]}, "item_1_description_1": {"attribute_name": "ID", "attribute_value_mlt": [{"subitem_description": "2006533", "subitem_description_type": "Other"}]}, "item_1_description_12": {"attribute_name": "要旨", "attribute_value_mlt": [{"subitem_description": "　　The　iron protoporphyrin IX（\u003ci\u003eb\u003c/i\u003e type heme）exists as a reaction center in most of the\u003cbr /\u003eheme proteins as a prosthetic group which bound with the protein matrix. 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}