{"created":"2023-07-27T06:50:25.376684+00:00","id":43192,"links":{},"metadata":{"_buckets":{"deposit":"78eaf269-0d1c-4bad-b357-76e585312667"},"_deposit":{"created_by":18,"id":"43192","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"43192"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00043192","sets":["934:935:937"]},"author_link":["2129","69594","638","69593"],"item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2018-06-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"3","bibliographicPageEnd":"290","bibliographicPageStart":"275","bibliographicVolumeNumber":"136","bibliographic_titles":[{"bibliographic_title":"Photosynthesis Research"}]}]},"item_4_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"瀨尾, 悌介"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"浅野, 智哉"}],"nameIdentifiers":[{},{},{}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Ferredoxin-NAD(P)+ reductase ([EC 1.18.1.2], [EC 1.18.1.3]) from Chlorobaculum tepidum (CtFNR) is structurally homologous to the bacterial NADPH-thioredoxin reductase (TrxR), but possesses a unique C-terminal extension relative to TrxR that interacts with the isoalloxazine ring moiety of the flavin adenine dinucleotide prosthetic group. In this study, we introduce truncations to the C-terminal residues to examine their role in the reactions of CtFNR with NADP+ and NADPH by spectroscopic and kinetic analyses. The truncation of the residues from Tyr326 to Glu360 (the whole C-terminal extension region), from Phe337 to Glu360 (omitting Phe337 on the re-face of the isoalloxazine ring) and from Ser338 to Glu360 (leaving Phe337 intact) resulted in a blue-shift of the flavin absorption bands. The truncations caused a slight increase in the dissociation constant toward NADP+ and a slight decrease in the Michaelis constant toward NADPH in steady-state assays. Pre-steady-state studies of the redox reaction with NADPH demonstrated that deletions of Tyr326–Glu360 decreased the hydride transfer rate, and the amount of reduced enzyme increased at equilibrium relative to wild-type CtFNR. In contrast, the deletions of Phe337–Glu360 and Ser338–Glu360 resulted in only slight changes in the reaction kinetics and redox equilibrium. These results suggest that the C-terminal region of CtFNR is responsible for the formation and stability of charge-transfer complexes, leading to changes in redox properties and reactivity toward NADP+/NADPH. © 2017 Springer Science+Business Media B.V., part of Springer Nature","subitem_description_type":"Abstract"}]},"item_4_description_22":{"attribute_name":"内容記述","attribute_value_mlt":[{"subitem_description":"Embargo Period 12 months","subitem_description_type":"Other"}]},"item_4_description_5":{"attribute_name":"提供者所属","attribute_value_mlt":[{"subitem_description":"金沢大学理工研究域物質化学系  ","subitem_description_type":"Other"}]},"item_4_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00049539","subitem_identifier_reg_type":"JaLC"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Springer Netherlands"}]},"item_4_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1007/s11120-017-0462-z","subitem_relation_type_select":"DOI"}}]},"item_4_rights_23":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"Copyright © 2017 Springer Science+Business Media B.V., part of Springer Nature"},{"subitem_rights":"The final publication is available at www.springerlink.com/article/10.1007/s11120-017-0462-z"}]},"item_4_source_id_11":{"attribute_name":"NCID","attribute_value_mlt":[{"subitem_source_identifier":"AA00362200","subitem_source_identifier_type":"NCID"}]},"item_4_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0166-8595","subitem_source_identifier_type":"ISSN"}]},"item_4_version_type_25":{"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":"Seo, Daisuke"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"Asano, Tomoya"}],"nameIdentifiers":[{},{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2019-06-02"}],"displaytype":"detail","filename":"SC-PR-SEO-D-2017.pdf","filesize":[{"value":"1.8 MB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"SC-PR-SEO-D-275.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/43192/files/SC-PR-SEO-D-2017.pdf"},"version_id":"5a54ee5a-ad01-4161-875c-951b3095ac24"}]},"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":"C-terminal residues of ferredoxin-NAD(P)+ reductase from Chlorobaculum tepidum are responsible for reaction dynamics in the hydride transfer and redox equilibria with NADP+/NADPH","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"C-terminal residues of ferredoxin-NAD(P)+ reductase from Chlorobaculum tepidum are responsible for reaction dynamics in the hydride transfer and redox equilibria with NADP+/NADPH"}]},"item_type_id":"4","owner":"18","path":["937"],"pubdate":{"attribute_name":"公開日","attribute_value":"2018-06-08"},"publish_date":"2018-06-08","publish_status":"0","recid":"43192","relation_version_is_last":true,"title":["C-terminal residues of ferredoxin-NAD(P)+ reductase from Chlorobaculum tepidum are responsible for reaction dynamics in the hydride transfer and redox equilibria with NADP+/NADPH"],"weko_creator_id":"18","weko_shared_id":-1},"updated":"2023-07-27T17:06:31.034029+00:00"}