{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T01:49:29Z","timestamp":1791510569251,"version":"4.3.4"},"reference-count":30,"publisher":"National Academy of Sciences","issue":"29","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2008,7,22]]},"abstract":"<jats:p>\n                    Cytochrome\n                    <jats:italic>c<\/jats:italic>\n                    oxidase (CcO) is a multimetallic enzyme that carries out the reduction of O\n                    <jats:sub>2<\/jats:sub>\n                    to H\n                    <jats:sub>2<\/jats:sub>\n                    O and is essential to respiration, providing the energy that powers all aerobic organisms by generating heat and forming ATP. The oxygen-binding heme a\n                    <jats:sub>3<\/jats:sub>\n                    should be subject to fatal inhibition by chemicals that could compete with O\n                    <jats:sub>2<\/jats:sub>\n                    binding. Near the CcO active site is another enzyme, NO synthase, which produces the gaseous hormone NO. NO can strongly bind to heme a\n                    <jats:sub>3<\/jats:sub>\n                    , thus inhibiting respiration. However, this disaster does not occur. Using functional models for the CcO active site, we show how NO inhibition is avoided; in fact, it is found that NO can protect the respiratory enzyme from other inhibitors such as cyanide, a classic poison.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0804257105","type":"journal-article","created":{"date-parts":[[2008,7,16]],"date-time":"2008-07-16T21:39:53Z","timestamp":1216244393000},"page":"9892-9896","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":53,"title":["Interaction of nitric oxide with a functional model of cytochrome\n                    <i>c<\/i>\n                    oxidase"],"prefix":"10.1073","volume":"105","author":[{"given":"James P.","family":"Collman","sequence":"first","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abhishek","family":"Dey","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard A.","family":"Decreau","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ying","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali","family":"Hosseini","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward I.","family":"Solomon","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Todd A.","family":"Eberspacher","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Stanford University, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2008,7,22]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr950051s"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/376660a0"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.280.5370.1723"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(77)90216-X"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(97)01397-5"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.18.11038"},{"key":"e_1_3_3_7_2","first-page":"274","article-title":"The toxic effects of cassava manihot esculenta grantz diets on humans: A review","volume":"33","author":"Aregheore EM","year":"1991","unstructured":"EM Aregheore, OO Agunbiade, The toxic effects of cassava manihot esculenta grantz diets on humans: A review. 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