{"created":"2023-05-15T14:59:12.830268+00:00","id":80341,"links":{},"metadata":{"_buckets":{"deposit":"b52c7997-201e-436f-973d-c70cfe89ec89"},"_deposit":{"created_by":1,"id":"80341","owners":[1],"pid":{"revision_id":0,"type":"depid","value":"80341"},"status":"published"},"_oai":{"id":"oai:repo.qst.go.jp:00080341","sets":["1"]},"author_link":["885977","885972","885978","885974","885979","885971","885975","885976","885980","885973","885981"],"item_8_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2020-04","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"5833","bibliographicPageStart":"5818","bibliographicVolumeNumber":"295","bibliographic_titles":[{"bibliographic_title":"Journal of Biological Chemistry"}]}]},"item_8_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Cytochrome c oxidase (CcO) reduces O2 to water, coupled with a proton-pumping process. The structure of the O2-reduction site of CcO contains two reducing equivalents, Fea32+ and CuB1+, and suggests that a peroxide-bound state (Fea33+–O−–O−–CuB2+) rather than an O2-bound state (Fea32+–O2) is the initial catalytic intermediate. Unexpectedly, however, resonance Raman spectroscopy results have shown that the initial intermediate is Fea32+–O2, whereas Fea33+–O−–O−–CuB2+ is undetectable. Based on X-ray structures of static noncatalytic CcO forms and mutation analyses for bovine CcO, a proton-pumping mechanism has been proposed. It involves a proton-conducting pathway (the H-pathway) comprising a tandem hydrogen-bond network and a water channel located between the N- and P-side surfaces. However, a system for unidirectional proton-transport has not been experimentally identified. Here, an essentially identical X-ray structure for the two catalytic intermediates (P and F) of bovine CcO was determined at 1.8 Å resolution. A 1.70 Å Fe–O distance of the ferryl center could best be described as Fea34+ = O2−, not as Fea34+–OH−. The distance suggests an ∼800-cm−1 Raman stretching band. We found an interstitial water molecule that could trigger a rapid proton-coupled electron transfer from tyrosine-OH to the slowly forming Fea33+–O−–O−–CuB2+ state, preventing its detection, consistent with the unexpected Raman results. The H-pathway structures of both intermediates indicated that during proton-pumping from the hydrogen-bond network to the P-side, a transmembrane helix closes the water channel connecting the N-side with the hydrogen-bond network, facilitating unidirectional proton-pumping during the P-to-F transition. ","subitem_description_type":"Abstract"}]},"item_8_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1074/jbc.RA119.009596","subitem_relation_type_select":"DOI"}}]},"item_8_relation_17":{"attribute_name":"関連サイト","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://www.jbc.org/content/295/17/5818.long","subitem_relation_type_select":"URI"}}]},"item_8_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0021-9258","subitem_source_identifier_type":"ISSN"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"metadata only access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_14cb"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Shimada, Atsuhiro"}],"nameIdentifiers":[{"nameIdentifier":"885971","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Etoh, Yuki"}],"nameIdentifiers":[{"nameIdentifier":"885972","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Rika Kitoh-Fujisawa"}],"nameIdentifiers":[{"nameIdentifier":"885973","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Sasaki, Ai"}],"nameIdentifiers":[{"nameIdentifier":"885974","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Kyoko, Shinzawa-Itoh"}],"nameIdentifiers":[{"nameIdentifier":"885975","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hiromoto, Takeshi"}],"nameIdentifiers":[{"nameIdentifier":"885976","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Eiki Yamashita"}],"nameIdentifiers":[{"nameIdentifier":"885977","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Muramoto, Kazumasa"}],"nameIdentifiers":[{"nameIdentifier":"885978","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Tsukihara, Tomitake"}],"nameIdentifiers":[{"nameIdentifier":"885979","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Shinya Yoshikawa"}],"nameIdentifiers":[{"nameIdentifier":"885980","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hiromoto, Takeshi","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"885981","nameIdentifierScheme":"WEKO"}]}]},"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":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms"}]},"item_type_id":"8","owner":"1","path":["1"],"pubdate":{"attribute_name":"公開日","attribute_value":"2020-08-19"},"publish_date":"2020-08-19","publish_status":"0","recid":"80341","relation_version_is_last":true,"title":["X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms"],"weko_creator_id":"1","weko_shared_id":-1},"updated":"2023-05-15T21:35:01.970335+00:00"}