{"id":68,"date":"2015-12-08T11:56:05","date_gmt":"2015-12-08T02:56:05","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=68"},"modified":"2025-01-22T11:15:16","modified_gmt":"2025-01-22T02:15:16","slug":"2000%e5%b9%b4%e4%bb%a5%e5%89%8d","status":"publish","type":"page","link":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/achievements\/2000%e5%b9%b4%e4%bb%a5%e5%89%8d\/","title":{"rendered":"2000\u5e74\u4ee5\u524d"},"content":{"rendered":"<h2 style=\"text-align: center\">~2000\u5e74<\/h2>\n<ul>\n<li>Akiyama, S.,\u00a0<u><strong>Takahashi, S<\/strong><\/u>.,Ishimori, K., Morishima, I. \u201cStepwise Formation of Alpha-Helices During Cytochrome c Folding\u201d Nat. Struct. Biol. 7, 514-520 (2000)\u00a0[<a href=\"http:\/\/www.nature.com\/nsmb\/journal\/v7\/n6\/full\/nsb0600_514.html\">Abstract<\/a>]<\/li>\n<li>Ihara, M., Shintaku, M.,<u>\u00a0<strong>Takahashi, S<\/strong>.<\/u>, Ishimori, K., Morishima, I. \u201cConversion of an Electron-Transfer Protein into an Oxygen Binding Protein: The Axial Cytochrome b5 Mutant with an Unusually High O2 Affinity\u201d J. Am. Chem. Soc. 122, 11535-11536 (2000)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja002914r\">Abstract<\/a>]<\/li>\n<li>Ihara, M.,<u>\u00a0<strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cFunctions of Fluctuation in the Heme-Binding Loops of Cytochrome b5 Revealed in the Process of Heme Incorporation\u201d Biochemistry 39, 5961-5970 (2000)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi9922289\">Abstract<\/a>]<\/li>\n<li>Yoshioka, S.,<u>\u00a0<strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cRoles of the Axial Push Effect in Cytochrome P450cam Studied with the Site-Directed Mutagenesis at the Heme Proximal Site\u201d J. Inorg. Biochem. 81, 141-151 (2000)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6TGG-417WD0D-3&amp;_user=127492&amp;_rdoc=1&amp;_fmt=&amp;_orig=search&amp;_sort=d&amp;_docanchor=&amp;view=c&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=24f0b27010fa21a4aacdfd3ac412ffd8\">Abstract<\/a>]<\/li>\n<li>Han, S.,\u00a0<u><strong>Takahashi, S<\/strong><\/u>., Rousseau, D. L. \u201cTime Dependence of the Catalytic Intermediates in Cytochrome c Oxidase\u201d J. Biol. Chem. 275, 1910-1919 (2000)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/275\/3\/1910?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=275&amp;firstpage=1910&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Sam, J. W., <u><strong>Takahashi, S<\/strong><\/u>., Lippai, I., Peisach, J., Rousseau, D. L. \u201cSequence-Specific Changes in the Metal Site of Ferric Bleomycin Induced by the Binding of DNA\u201d J. Biol. Chem. 273, 16090-16097 (1998).[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/273\/26\/16090?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=273&amp;firstpage=16090&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Zamparelli, C., Verzili, D., Boffi, A., Chiancone, E., <u><strong>Takahashi, S<\/strong><\/u>., Rousseau, D. L., Regan, R., Gibson, Q. H. \u201cThe Unique Heme-Heme Interactions of the Homodimeric Scapharca Inaequivalvis Hemoglobin as Probed in the Protein Reconstituted with Unnatural 2,4 Heme Derivatives\u201d<br \/>\nArch. Biochem. Biophys. 339, 275-282 (1997)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WB5-45MH19S-FG&amp;_user=127492&amp;_rdoc=1&amp;_fmt=&amp;_orig=search&amp;_sort=d&amp;_docanchor=&amp;view=c&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=7c90d8f9483e58f7617725d50f784bc5\">Abstract<\/a>]<\/li>\n<li>Chan, C. K., Hu, Y., <u><strong>Takahashi, S<\/strong><\/u>., Rousseau, D. L., Eaton, W. A., Hofrichter, J. \u201cSubmillisecond Protein Folding Kinetics Studied by Ultrarapid Mixing\u201d Proc. Natl. Acad. Sci. U. S. A. 94, 1779-1784 (1997)\u00a0[<a href=\"http:\/\/www.pnas.org\/gca?gca=pnas%3B94%2F5%2F1779&amp;allch=\">Abstract<\/a>]<\/li>\n<li>Boffi, A., Chiancone, E., <u><strong>Takahashi, S<\/strong><\/u>., Rousseau, D. L. \u201cStereochemistry of the Fe(II)- and Fe(III)-Cyanide Complexes of the Homodimeric Scapharca Inaequivalvis Hemoglobin. A Resonance Raman and FTIR Study\u201d Biochemistry36, 4505-4509 (1997)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi9618880\">Abstract<\/a>]<\/li>\n<li>Yeh, S. R., <u><strong>Takahashi, S<\/strong><\/u>., Fan, B. C., Rousseau, D. L. \u201cLigand Exchange During Cytochrome c Folding\u201d Nat. Struct. Biol. 4, 51-56 (1997)\u00a0[<a href=\"http:\/\/www.nature.com\/nsmb\/journal\/v4\/n1\/abs\/nsb0197-51.html\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>., Yeh, S. R., Das, T. K., Chan, C. K., Gottfried, D. S., Rousseau, D. L. \u201cFolding of Cytochrome c Initiated by Submillisecond Mixing\u201d Nat. Struct. Biol. 4, 44-50 (1997)\u00a0[<a href=\"http:\/\/www.nature.com\/nsmb\/journal\/v4\/n1\/abs\/nsb0197-44.html\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>., Matera, K. M., Fujii, H., Zhou, H., Ishikawa, K., Yoshida, T., Ikedasaito, M., Rousseau, D. L. \u201cResonance Raman Spectroscopic Characterization of Alpha-Hydroxyheme and Verdoheme Complexes of Heme Oxygenase\u201d Biochemistry36, 1402-1410 (1997)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi962361q\">Abstract<\/a>]<\/li>\n<li>Matera, K. M., <u><strong>Takahashi, S<\/strong><\/u>., Fujii, H., Zhou, H., Ishikawa, K., Yoshimura, T., Rousseau, D. L., Yoshida, T., Ikedasaito, M. \u201cOxygen and One Reducing Equivalent Are Both Required for the Conversion of Alpha-Hydroxyhemin to Verdoheme in Heme Oxygenase\u201d J. Biol. Chem. 271, 6618-6624 (1996) [<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/271\/12\/6618?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=271&amp;firstpage=6618&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Wang, J. L., <u><strong>Takahashi, S<\/strong><\/u>., Hosler, J. P., Mitchell, D. M., Fergusonmiller, S., Gennis, R. B., Rousseau, D. L. \u201cTwo Conformations of the Catalytic Site in the aa3-Type Cytochrome c Oxidase from Rhodobacter Sphaeroides\u201d Biochemistry34, 9819-9825 (1995)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi00031a001\">Abstract<\/a>]<\/li>\n<li>Wang, J. L., <u><strong>Takahashi, S<\/strong><\/u>., Rousseau, D. L. \u201cIdentification of the Overtone of the Fe-CO Stretching Mode in Heme-Proteins &#8211; a Probe of the Heme Active-Site\u201d Proc. Natl. Acad. Sci. U. S. A. 92, 9402-9406 (1995) [<a href=\"http:\/\/www.pnas.org\/gca?allch=&amp;gca=pnas%3B92%2F20%2F9402\">Abstract<\/a>]<\/li>\n<\/ul>\n<ul>\n<li>Wang, J. L., Rumbley, J., Ching, Y. C., <u><strong>Takahashi, S<\/strong><\/u>., Gennis, R. B., Rousseau, D. L. \u201cReaction of Cytochrome bo3 with Oxygen &#8211; Extra Redox Center(s) Are Present in the Protein\u201d Biochemistry34, 15504-15511 (1995)[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi00047a016\">Abstract<\/a>]<\/li>\n<li>Ishikawa, K., Takeuchi, N., <u><strong>Takahashi, S<\/strong><\/u>., Matera, K. M., Sato, M., Shibahara, S., Rousseau, D. L., Ikedasaito, M., Yoshida, T. \u201cHeme Oxygenase-2 &#8211; Properties of the Heme Complex of the Purified Tryptic Fragment of Recombinant Human Heme Oxygenase-2\u201d J. Biol. Chem. 270, 6345-6350 (1995)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/270\/11\/6345?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=270&amp;firstpage=6345&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>., Ching, Y. C., Wang, J. L., Rousseau, D. L. \u201cMicrosecond Generation of Oxygen-Bound Cytochrome c Oxidase by Rapid Solution Mixing\u201d J. Biol. Chem. 270, 8405-8407 (1995)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/270\/15\/8405?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=270&amp;firstpage=8405&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>., Ishikawa, K., Takeuchi, N., Ikedasaito, M., Yoshida, T., Rousseau, D. L. \u201cOxygen-Bound Heme-Heme Oxygenase Complex &#8211; Evidence for a Highly Bent Structure of the Coordinated Oxygen\u201d J.Am. Chem. Soc. 117, 6002-6006 (1995) [<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja00127a013\">Abstract<\/a>]<\/li>\n<li>Boffi, A., <u><strong>Takahashi, S<\/strong><\/u>., Spagnuolo, C., Rousseau, D. L., Chiancone, E. \u201cStructural Characterization of Oxidized Dimeric Scapharca- Inaequivalvis Hemoglobin by Resonance Raman-Spectroscopy\u201dJ. Biol. Chem. 269, 20437-20440 (1994)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/269\/32\/20437?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=269&amp;firstpage=20437&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>., Sam, J. W., Peisach, J., Rousseau, D. L. \u201cStructural Characterization of Iron-Bleomycin by Resonance Raman-Spectroscopy\u201d J. Am. Chem. Soc. 116, 4408-4413 (1994) [<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja00089a032\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>. , Wang, J. L., Rousseau, D. L., Ishikawa, K., Yoshida, T., Takeuchi, N., Ikedasaito, M.<br \/>\n\u201cHeme-Heme Oxygenase Complex &#8211; Structure and Properties of the Catalytic Site from Resonance Raman-Scattering\u201d Biochemistry 33, 5531-5538 (1994) [<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi00184a023\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>. , Wang, J. L., Rousseau, D. L., Ishikawa, K., Yoshida, T., Host, J. R.,Ikedasaito, M.<br \/>\n\u201cHeme-Heme Oxygenase Complex Structure of the Catalytic Site and Its Implication for Oxygen Activation\u201d J. Biol. Chem. 269, 1010-1014 (1994) [<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/269\/2\/1010?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=269&amp;firstpage=1010&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Yumoto, I., <u><strong>Takahashi, S<\/strong><\/u>., Kitagawa, T., Fukumori, Y., Yamanaka, T. \u201cThe Molecular-Features and Catalytic Activity of CuA-Containing aco3-Type Cytochrome c Oxidase from a Facultative Alkalophilic Bacillus\u201d J. Biochem. (Tokyo) 114, 88-95 (1993)\u00a0[<a href=\"http:\/\/jb.oxfordjournals.org\/cgi\/reprint\/114\/1\/88\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>. , Ogura, T., Shinzawa-Itoh, K., Yoshikawa, S., Kitagawa, T. \u201cResonance Raman Studies on the CuA Site of Cytochrome c Oxidase Using a Multichannel Scanning Raman Spectrometer with a CCD Detector\u201d Biochemistry 32, 3664-3670 (1993)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi00065a020\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>. , Ahn, J. S., Asaka, S., Kitagawa, T. \u201cMultichannel Fourier-Transform Spectroscopy Using Two-Dimensional Detection of the Interferogram and Its Application to Raman- Spectroscopy\u201d Appl. Spectrosc. 47, 863-868 (1993)<\/li>\n<li>Ogura, T.,<u> <strong>Takahashi, S<\/strong><\/u>., Hirota, S., Shinzawa-Itoh, K., Yoshikawa, S., Appelman, E. H., Kitagawa, T. \u201cTime-Resolved Resonance Raman Elucidation of the Pathway for Dioxygen Reduction by Cytochrome-c-Oxidase\u201d J. Am. Chem. Soc. 115, 8527-8536 (1993)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja00072a002\">Abstract<\/a>]<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>. , Ogura, T., Itoh-Shinzawa, K., Yoshikawa, S., Kitagawa, T.<br \/>\n\u201cObservation of the CuA-Ligand Stretching Resonance Raman Band for Cytochrome c Oxidase\u201d<br \/>\nJ. Am. Chem. Soc. 113, 9400-9401 (1991)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja00024a073\">Abstract]<\/a><\/li>\n<li>Ogura, T., <u><strong>Takahashi, S<\/strong><\/u>., Shinzawa-Itoh, K., Yoshikawa, S., Kitagawa, T. \u201cTime-Resolved Resonance Raman Investigation of Cytochrome Oxidase Catalysis &#8211; Observation of a New Oxygen-Isotope Sensitive Raman Band\u201d Bull. Chem. Soc. Jpn. 64, 2901-2907 (1991)<\/li>\n<li>Ogura, T., <u><strong>Takahashi, S<\/strong><\/u>., Shinzawa-Itoh, K., Yoshikawa, S., Kitagawa, T. \u201cObservation of the Fe(II)-O2 Stretching Raman Band for Cytochrome Oxidase Compound A at Ambient-Temperature\u201d<br \/>\nJ. Am. Chem. Soc. 112, 5630-5631 (1990)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja00170a032\">Abstract<\/a>]<\/li>\n<li>Ogura, T., <u><strong>Takahashi, S<\/strong><\/u>., Shinzawa-Itoh, K., Yoshikawa, S., Kitagawa, T. \u201cObservation of the Fe4+=O Stretching Raman Band for Cytochrome Oxidase Compound B at Ambient-Temperature\u201d J. Biol. Chem. 265, 14721-14723 (1990)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/265\/25\/14721?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=265&amp;firstpage=14721&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Sakata, T., <u><strong>Takahashi, S<\/strong><\/u>., Terazima, M., Azumi, T. \u201cMeasurement of the Enhancement Factor of Chemically-Induced Dynamic Nuclear-Polarization in the Photolysis of Dibenzyl Ketone &#8211; Determination of the Spin Multiplicity of the Precursor\u201d J. Phys. Chem. 95, 8671-8676 (1991)<\/li>\n<li>Terazima, M., Maeda, K., Sugawara, M., <u><strong>Takahashi, S<\/strong><\/u>., Azumi, T. \u201cCIDEP and CIDNP Studies of the Hydrogen Abstraction of 9,10- Anthraquinone from Xanthene\u201d J. Chem. Soc.-Faraday Trans. 86, 253-256 (1990)<\/li>\n<li><u><strong>Takahashi, S<\/strong><\/u>., Terazima, M., Azumi, T. \u201cTemperature-Dependence of the Enhancement Factor of CIDNP Created by the Photolysis of Benzoyl Peroxide\u201d Chem. Phys. 142, 69-74 (1990)<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>~2000\u5e74 Akiyama, S.,\u00a0Takahashi, S.,Ishimori, K., Morishima, I. &#8230;<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":37,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-68","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/68","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/comments?post=68"}],"version-history":[{"count":4,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/68\/revisions"}],"predecessor-version":[{"id":1094,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/68\/revisions\/1094"}],"up":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/37"}],"wp:attachment":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/media?parent=68"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}