{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:22:52Z","timestamp":1781108572032,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1971,12]]},"abstract":"<jats:p>\n                    An active\n                    <jats:italic>Neurospora<\/jats:italic>\n                    -like assimilatory NADPH-nitrate reductase (EC 1.6.6.2), which can be formed\n                    <jats:italic>in vitro<\/jats:italic>\n                    by incubation of extracts of nitrate-induced\n                    <jats:italic>Neurospora crassa<\/jats:italic>\n                    mutant\n                    <jats:italic>nit-1<\/jats:italic>\n                    with extracts of (\n                    <jats:italic>a<\/jats:italic>\n                    ) certain other nonallelic nitrate reductase mutants, (\n                    <jats:italic>b<\/jats:italic>\n                    ) uninduced wild type, or (\n                    <jats:italic>c<\/jats:italic>\n                    ) xanthine oxidizing and liver aldehyde-oxidase systems was also formed by combination of the\n                    <jats:italic>nit-1<\/jats:italic>\n                    extract with other acid-treated enzymes known to contain molybdenum. These molybdenum enzymes included (\n                    <jats:italic>a<\/jats:italic>\n                    ) nitrogenase, or its molybdenum-iron protein, from\n                    <jats:italic>Clostridium, Azotobacter<\/jats:italic>\n                    , and soybeannodule bacteroids, (\n                    <jats:italic>b<\/jats:italic>\n                    ) bovine liver sulfite oxidase, (\n                    <jats:italic>c<\/jats:italic>\n                    ) respiratory formate-nitrate reductase from\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    , (\n                    <jats:italic>d<\/jats:italic>\n                    ) NADH-nitrate reductase from foxtail grass (\n                    <jats:italic>Setaria faberii<\/jats:italic>\n                    ), and (\n                    <jats:italic>e<\/jats:italic>\n                    ) FADH\n                    <jats:sub>2<\/jats:sub>\n                    - and reduced methyl viologennitrate reductase preparations from certain\n                    <jats:italic>Neurospora<\/jats:italic>\n                    mutants. Several molybdenum-amino-acid complexes, as possible catalytic models of nitrogenase, were inactive (as were some previously tested 20 nonmolybdenum enzymes) in place of the acid-treated molybdenum-containing enzymes. The results imply the existence of a molybdenum-containing component shared by the known molybdenum-enzymes.\n                  <\/jats:p>","DOI":"10.1073\/pnas.68.12.3242","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T02:27:16Z","timestamp":1149042436000},"page":"3242-3246","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":162,"title":["<i>In Vitro<\/i>\n                    Formation of Assimilatory Reduced Nicotinamide Adenine Dinucleotide Phosphate: Nitrate Reductase from a\n                    <i>Neurospora<\/i>\n                    Mutant and a Component of Molybdenum-Enzymes"],"prefix":"10.1073","volume":"68","author":[{"given":"Alvin","family":"Nason","sequence":"first","affiliation":[{"name":"McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kuo-Yung","family":"Lee","sequence":"additional","affiliation":[{"name":"McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Su-Shu","family":"Pan","sequence":"additional","affiliation":[{"name":"McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul A.","family":"Ketchum","sequence":"additional","affiliation":[{"name":"McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio","family":"Lamberti","sequence":"additional","affiliation":[{"name":"McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"DeVries","sequence":"additional","affiliation":[{"name":"McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1971,12]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.68.12.3242","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T10:35:17Z","timestamp":1649846117000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.68.12.3242"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1971,12]]},"references-count":0,"journal-issue":{"issue":"12","published-print":{"date-parts":[[1971,12]]}},"alternative-id":["10.1073\/pnas.68.12.3242"],"URL":"https:\/\/doi.org\/10.1073\/pnas.68.12.3242","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1971,12]]},"assertion":[{"value":"1971-12-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}