{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:25:07Z","timestamp":1781105107525,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"9","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1972,9]]},"abstract":"<jats:p>\n                    The decarboxylation of DOPA by erythrocyte hemolysates differs from DOPA decarboxylation catalyzed by aromatic aminoacid decarboxylases that contain vitamin B\n                    <jats:sub>6<\/jats:sub>\n                    in several significant respects. The ability of erythrocyte hemolysates to decarboxylate DOPA is associated with interaction between DOPA and methemoglobin; the ferriheme protein is reduced and DOPA is decarboxylated, probably after oxidation to a quinone intermediate. An analogous reaction takes place between DOPA and other ferriheme proteins, such as metmyoglobin and cytochrome\n                    <jats:italic>c<\/jats:italic>\n                    . This phenomenon may be of significance in relation to the side effects observed in patients with Parkinson's disease who are treated with very large doses of DOPA.\n                  <\/jats:p>","DOI":"10.1073\/pnas.69.9.2505","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T02:38:45Z","timestamp":1149043125000},"page":"2505-2508","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":9,"title":["Decarboxylation of 3,4-Dihydroxyphenylalanine (DOPA) by Erythrocytes: A Reaction Promoted by Methemoglobin and Other Ferriheme Proteins"],"prefix":"10.1073","volume":"69","author":[{"given":"Suresh S.","family":"Tate","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Cornell University Medical College, New York, N.Y. 10021"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph","family":"Orlando","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Cornell University Medical College, New York, N.Y. 10021"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alton","family":"Meister","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Cornell University Medical College, New York, N.Y. 10021"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1972,9]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.69.9.2505","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T10:50:01Z","timestamp":1649847001000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.69.9.2505"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1972,9]]},"references-count":0,"journal-issue":{"issue":"9","published-print":{"date-parts":[[1972,9]]}},"alternative-id":["10.1073\/pnas.69.9.2505"],"URL":"https:\/\/doi.org\/10.1073\/pnas.69.9.2505","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1972,9]]},"assertion":[{"value":"1972-09-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}