{"_buckets": {"deposit": "f7bbebc0-bd39-4c70-a6a2-a3629152643c"}, "_deposit": {"created_by": 1, "id": "261", "owners": [1], "pid": {"revision_id": 0, "type": "depid", "value": "261"}, "status": "published"}, "_oai": {"id": "oai:ir.soken.ac.jp:00000261", "sets": ["10"]}, "author_link": ["7929", "7930", "7928"], "item_1_biblio_info_21": {"attribute_name": "書誌情報（ソート用）", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "1992-09-28", "bibliographicIssueDateType": "Issued"}, "bibliographic_titles": [{}]}]}, "item_1_creator_2": {"attribute_name": "著者名", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "目, 喜直"}], "nameIdentifiers": [{"nameIdentifier": "7928", "nameIdentifierScheme": "WEKO"}]}]}, "item_1_creator_3": {"attribute_name": "フリガナ", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "サカン, ヨシナオ"}], "nameIdentifiers": [{"nameIdentifier": "7929", "nameIdentifierScheme": "WEKO"}]}]}, "item_1_date_granted_11": {"attribute_name": "学位授与年月日", "attribute_value_mlt": [{"subitem_dategranted": "1992-09-28"}]}, "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": "1992505", "subitem_description_type": "Other"}]}, "item_1_description_12": {"attribute_name": "要旨", "attribute_value_mlt": [{"subitem_description": "　　Myoglobin(Mb) that is monomer and Hemoglobin(Hb) that is\n tetramer are one of the most basic hemoproteins. Hb has a Physiological\n function as an oxygen carrier in blood, and Mb can store oxygen in mus-\ncle. Both of Mb and a subunit of Hb consist of one heme (iron protopor-\nphtrin IX) and a single polypeptide chain.Mb and Hb bind carbonmonox-\nide(CO) at the oxygen binding site. Carbonmonoxy myoglobin (MbCO)\nand carbonmonoxy hemoglobin (HbCO) are photodissociable upon laser\n illumination,reversibly.\n　　According to the x-ray data of crystalline Mb,there is no pathway\nfor the ligand entry from the solvent to the heme pocket. However,in\nsome of derivative Mb another structure was also detected, in which distal\n histidine swings out toward the solvent and a pathway for the ligand entry\n is open. This structure is called \"open\"form, and the other structure that\n has no pathway is called \"closed\" form. When the ligand enters into the\n heme pocket , it is expected that the protein around the heme undergoes\n the conformational change. On the other hand, IR and Raman spectros-\ncopy showed that in acidic MbCO, the C-O(v\u003csmall\u003ec-o\u003c/small\u003e) and Fe-CO(v\u003csmall\u003eFe-co\u003c/small\u003e)\n stretchinig vibrational modes are located at different frequencies from\n these of neutral MbCO. In the present Raman experiment two v\u003csmall\u003eFe-co\u003c/small\u003e\n bands were identified at around 490 cm\u003csup\u003e-1\u003c/sup\u003e and 510 cm\u003csup\u003e-1\u003c/sup\u003e for MbCO at pH\n 4.5, while only one peak was observed at 510 cm\u003csup\u003e-1\u003c/sup\u003e for MbCO at neutral\n pH. The value pH 4.5 happens to be equal to the pK\u003csmall\u003ea\u003c/small\u003e value of the distal\n histidine and thus, half of the distal histidine is protonated at pH 4.5.\nTherefore, it was inferred that the protonated distal histidine repelled\n lysine-45 in the vicinity of the heme distal side, and the protein conforma-\ntion changed to the \"open\" form. Thus, the higher and lower frequency of\n v\u003csmall\u003eFe-co\u003c/small\u003e correspond to the \"closed\" and \"open\" form, respectively. The v\u003csmall\u003eFe-\u003c/small\u003e\n\u003csmall\u003eco\u003c/small\u003efrequency is sensitive to the Fe-C-O angle. According to the XANES\n of MbCO solution at neutral pH, the Fe-C-O bent angle is 150. From a\n simple normal-coordinate calculation for isolated three-body oscillators,\nthe v\u003csmall\u003eFe-co\u003c/small\u003e frequencies for the bent angle of 160 and 180 were estimated\n at 500 cm\u003csup\u003e-1\u003c/sup\u003e and 490 cm\u003csup\u003e-1\u003c/sup\u003e, respectively. It is assumed that the Fe-C-O\n angle of the \"open\" form is linear and that of \"closed\" form is bent.\n　　If the photodissociated ligand recombines to the \"open\" form and\n relaxes to the \"closed\" form gradually at neutral pH, the v\u003csmall\u003eFe-co\u003c/small\u003e should\n appear around 490 cm\u003csup\u003e-1\u003c/sup\u003e first and shift to 505 cm\u003csup\u003e-1\u003c/sup\u003e. In this study, the\n nanosecond time-resolved resonance Ranman(TR\u003csup\u003e3\u003c/sup\u003e) spectra were ob-\nserved in order to catch the transient species of MbCO on the recombina-\ntion reaction. TR\u003csup\u003e3\u003c/sup\u003e spectroscopy is a powerful technique to analyze the\n dynamical conformation in short time scale, and information obtained by it\n is very basic and important in studies of the relationship between physio-\nlogical functions and protein dynamics.\n　　MbCO at acidic pH(4.5), containing equal amounts of the \"closed\"\n and the \"open\" forms, were measured by the TR\u003csup\u003e3\u003c/sup\u003e system. If the assump-\ntion above is true, the recombination rate of the \"open\" form should be\n faster than that of the \"closed\" form. Indeed, the temporal behaviors of the\n v\u003csmall\u003eFe-co\u003c/small\u003e bands of the \"open\" and \"closed\" forms were different. The v\u003csmall\u003eFe-co\u003c/small\u003e\n band of the \"open\" form recovered faster than the \"closed\" form. Howev-\ner, at neutral pH, there were no transient bands around 490 cm\u003csup\u003e-1\u003c/sup\u003e in all\n time range observed (-20ns-1ms). It suggests either that the transient\n \"open\" form is absent or that the structural is change too fast to be detect\ned(ChapterII).\n　　In the acide pH,the recombination kinetics may be affected by pH\n effect. It is desirable to measure both of \"open\" and \"closed\" forms under\n identical conditions including pH and temperatures. The human abnormal\n hemoglobins, \"Boston\" and \"Saskatoon\" are best models for this purpose,\n since abnormal hemoglobins contain two types subunits in one molecule,\nthat is normal chains and abnormal chains. In the abnormal chain the\n distal histidine is replaced by tyrosine. In \"Boston\", the α-chain is abnor-\nmal, and in \"Saskatoon\" the β-chain is abnormal. Their v\u003csmall\u003eFe-co\u003c/small\u003e bands\n arise around 490 and 505 cm\u003csup\u003e-1\u003c/sup\u003e, corresponding to the \"open\" and \"closed\"\n forms, respectively (ChapterIII).\n　　Some human MbCO mutants whose distal His was replaced by\n various amino acids residues through site-directed mutagenesis were\n also examined at neutral pH in order to make clarity the role of the distal\n histidine on the rebinding reaction. Some of them have the v\u003csmal\u003eFe-co\u003c/small\u003e band\n around 490 cm\u003csup\u003e-1\u003c/sup\u003e and the others have it around 510 cm\u003csup\u003e-1\u003c/sup\u003e (ChapterIV).\n  The results from the experiments on these Hbs and Mbs also showed that\n MbCO with the lower v\u003csmall\u003eFe-co\u003c/small\u003e band recovered faster than that with higher\n band. Transient bands observed the time range between 100-1000ns\n were significantly broad. The transient \"open\" form was not detected in all\n time range for the species with the \"closed\" equilibrium structure. These\n results suggested that the ligand enterd to the heme pocket through a\n pathway which was created by a conformational changes in the distal side,\n but the so-called \"open\" form was never produced during the recombina-\ntion reaction. The Fe-C-O angle in a transient form seems to be slightly\n perturbed around the equilibrium angle and it has appreciable distribu-\ntions.", "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36号", "subitem_description_type": "Other"}]}, "item_1_select_14": {"attribute_name": "所蔵", "attribute_value_mlt": [{"subitem_select_item": "有"}]}, "item_1_select_16": {"attribute_name": "複写", "attribute_value_mlt": [{"subitem_select_item": "全文複写可"}]}, "item_1_select_17": {"attribute_name": "公開状況", "attribute_value_mlt": [{"subitem_select_item": "全文公開可"}]}, "item_1_select_8": {"attribute_name": "研究科", "attribute_value_mlt": [{"subitem_select_item": "数物科学研究科"}]}, "item_1_select_9": {"attribute_name": "専攻", "attribute_value_mlt": [{"subitem_select_item": "08 機能分子科学専攻"}]}, "item_1_text_10": {"attribute_name": "学位授与年度", "attribute_value_mlt": [{"subitem_text_value": "1992"}]}, "item_1_text_20": {"attribute_name": "業務メモ", "attribute_value_mlt": [{"subitem_text_value": "（2017年11月21日）本籍など個人情報の記載がある旧要旨・審査要旨を個人情報のない新しいものに差し替えた。承諾書を確認した。学位規則変更前のため、本文は国会図書館の自動収集対象外（製本納入）なので、著者版フラグはauthorにする。"}]}, "item_1_version_type_23": {"attribute_name": "著者版フラグ", "attribute_value_mlt": [{"subitem_version_resource": "http://purl.org/coar/version/c_ab4af688f83e57aa", "subitem_version_type": "AM"}]}, "item_creator": {"attribute_name": "著者", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "SAKAN, Yoshinao", "creatorNameLang": "en"}], "nameIdentifiers": [{"nameIdentifier": "7930", "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36_要旨.pdf", "filesize": [{"value": "370.0 kB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_11", "mimetype": "application/pdf", "size": 370000.0, "url": {"label": "要旨・審査要旨 / Abstract, Screening Result", "url": "https://ir.soken.ac.jp/record/261/files/甲36_要旨.pdf"}, "version_id": "ca0e892e-167b-490d-ac54-7ab63e29fc37"}, {"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2016-02-17"}], "displaytype": "simple", "download_preview_message": "", "file_order": 1, "filename": "甲36_本文.pdf", "filesize": [{"value": "2.7 MB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_11", "mimetype": "application/pdf", "size": 2700000.0, "url": {"label": "本文 / Thesis", "url": "https://ir.soken.ac.jp/record/261/files/甲36_本文.pdf"}, "version_id": "c2e3b06f-1a51-46d2-a3af-6733018f941e"}]}, "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": "時間分解共鳴ラマン分光法による光解離後の一酸化炭素結合型ミオグロビンとヘモグロビンのタンパク質動的構造の研究", "item_titles": {"attribute_name": "タイトル", "attribute_value_mlt": [{"subitem_title": "時間分解共鳴ラマン分光法による光解離後の一酸化炭素結合型ミオグロビンとヘモグロビンのタンパク質動的構造の研究"}, {"subitem_title": "Studies on the Protein Dynamics of Photodissociated Carbonmonoxy Myoglobin and Hemoglobin by Time-Resolved Resonance Raman Spectroscopy", "subitem_title_language": "en"}]}, "item_type_id": "1", "owner": "1", "path": ["10"], "permalink_uri": "https://ir.soken.ac.jp/records/261", "pubdate": {"attribute_name": "公開日", "attribute_value": "2010-02-22"}, "publish_date": "2010-02-22", "publish_status": "0", "recid": "261", "relation": {}, "relation_version_is_last": true, "title": ["時間分解共鳴ラマン分光法による光解離後の一酸化炭素結合型ミオグロビンとヘモグロビンのタンパク質動的構造の研究"], "weko_shared_id": 1}