Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing
Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derive...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2020-05, Vol.117 (20), p.10818-10824 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Murakawa, Takeshi Kurihara, Kazuo Shoji, Mitsuo Shibazaki, Chie Sunami, Tomoko Tamada, Taro Yano, Naomine Yamada, Taro Kusaka, Katsuhiro Suzuki, Mamoru Shigeta, Yasuteru Kuroki, Ryota Hayashi, Hideyuki Yano, Takato Tanizawa, Katsuyuki Adachi, Motoyasu Okajima, Toshihide |
| description | Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions. |
| doi_str_mv | 10.1073/pnas.1922538117 |
| format | Article |
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Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1922538117</identifier><identifier>PMID: 32371483</identifier><language>eng</language><publisher>WASHINGTON: National Academy of Sciences</publisher><subject>Biological Sciences ; Copper ; Crystal structure ; Crystallography ; Histidine ; Multidisciplinary Sciences ; Oxidase ; Prostheses ; Protonation ; Protons ; Quinones ; Science & Technology ; Science & Technology - Other Topics</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2020-05, Vol.117 (20), p.10818-10824</ispartof><rights>Copyright National Academy of Sciences May 19, 2020</rights><rights>2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>10</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000535585100034</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c553t-93ab3228c2fa41f18689ec0fd16b8a9b5292792b150e3a11ff6e206c2efe4c783</citedby><cites>FETCH-LOGICAL-c553t-93ab3228c2fa41f18689ec0fd16b8a9b5292792b150e3a11ff6e206c2efe4c783</cites><orcidid>0000-0003-1419-8022 ; 0000-0001-5905-532X ; 0000-0003-0695-2187 ; 0000-0002-3219-6007 ; 0000-0001-7465-6326 ; 0000-0002-9720-8339 ; 0000-0003-1733-9580 ; 0000-0001-9774-6885 ; 0000-0002-4073-3028</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/26931142$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/26931142$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27929,27930,28253,53796,53798,58022,58255</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32371483$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murakawa, Takeshi</creatorcontrib><creatorcontrib>Kurihara, Kazuo</creatorcontrib><creatorcontrib>Shoji, Mitsuo</creatorcontrib><creatorcontrib>Shibazaki, Chie</creatorcontrib><creatorcontrib>Sunami, Tomoko</creatorcontrib><creatorcontrib>Tamada, Taro</creatorcontrib><creatorcontrib>Yano, Naomine</creatorcontrib><creatorcontrib>Yamada, Taro</creatorcontrib><creatorcontrib>Kusaka, Katsuhiro</creatorcontrib><creatorcontrib>Suzuki, Mamoru</creatorcontrib><creatorcontrib>Shigeta, Yasuteru</creatorcontrib><creatorcontrib>Kuroki, Ryota</creatorcontrib><creatorcontrib>Hayashi, Hideyuki</creatorcontrib><creatorcontrib>Yano, Takato</creatorcontrib><creatorcontrib>Tanizawa, Katsuyuki</creatorcontrib><creatorcontrib>Adachi, Motoyasu</creatorcontrib><creatorcontrib>Okajima, Toshihide</creatorcontrib><title>Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>P NATL ACAD SCI USA</addtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. 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| subjects | Biological Sciences Copper Crystal structure Crystallography Histidine Multidisciplinary Sciences Oxidase Prostheses Protonation Protons Quinones Science & Technology Science & Technology - Other Topics |
| title | Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing |
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