{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,27]],"date-time":"2025-09-27T17:00:10Z","timestamp":1758992410352},"reference-count":18,"publisher":"American Chemical Society (ACS)","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Am. Chem. Soc."],"published-print":{"date-parts":[[1999,3,1]]},"DOI":"10.1021\/ja9841761","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T05:34:40Z","timestamp":1027661680000},"page":"2625-2626","source":"Crossref","is-referenced-by-count":37,"title":["Observation of Ligand-Based Redox Chemistry at the Active Site of a Molybdenum Enzyme"],"prefix":"10.1021","volume":"121","author":[{"given":"Graham N.","family":"George","sequence":"first","affiliation":[{"name":"Stanford Synchrotron Radiation Laboratory, SLAC Stanford University, PO Box 4349, MS 69 Stanford, California 94309 Departmento de Qu\u00edmica Centro de Qu\u00edmica Fina e Biotecnologia Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa 2825 Monte de Caparica, Portugal"}]},{"given":"Cristina","family":"Costa","sequence":"additional","affiliation":[{"name":"Stanford Synchrotron Radiation Laboratory, SLAC Stanford University, PO Box 4349, MS 69 Stanford, California 94309 Departmento de Qu\u00edmica Centro de Qu\u00edmica Fina e Biotecnologia Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa 2825 Monte de Caparica, Portugal"}]},{"given":"Jos\u00e9 J. G.","family":"Moura","sequence":"additional","affiliation":[{"name":"Stanford Synchrotron Radiation Laboratory, SLAC Stanford University, PO Box 4349, MS 69 Stanford, California 94309 Departmento de Qu\u00edmica Centro de Qu\u00edmica Fina e Biotecnologia Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa 2825 Monte de Caparica, Portugal"}]},{"given":"Isabel","family":"Moura","sequence":"additional","affiliation":[{"name":"Stanford Synchrotron Radiation Laboratory, SLAC Stanford University, PO Box 4349, MS 69 Stanford, California 94309 Departmento de Qu\u00edmica Centro de Qu\u00edmica Fina e Biotecnologia Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa 2825 Monte de Caparica, Portugal"}]}],"member":"316","published-online":{"date-parts":[[1999,3,9]]},"reference":[{"key":"ja9841761b00001\/ja9841761b00001_1","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.biochem.66.1.233","volume":"66","author":"Kisker C.","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"ja9841761b00001\/ja9841761b00001_2","doi-asserted-by":"crossref","first-page":"2816","DOI":"10.1021\/cr950061t","volume":"96","author":"Hille R.","year":"1996","journal-title":"Chem. Rev."},{"key":"ja9841761b00002\/ja9841761b00002_1","doi-asserted-by":"crossref","first-page":"2859","DOI":"10.1021\/cr950063d","volume":"96","author":"Johnson M. K.","year":"1996","journal-title":"Chem. Rev."},{"key":"ja9841761b00003\/ja9841761b00003_1","doi-asserted-by":"crossref","DOI":"10.1128\/jb.177.20.5767-5772.1995","volume":"177","author":"Rosner B. M.","year":"1995","journal-title":"J. Bacteriol."},{"key":"ja9841761b00004\/ja9841761b00004_1","first-page":"3528","volume":"37","author":"Khangulov S. V.","year":"1998","journal-title":"Biochemistry"},{"key":"ja9841761b00005\/ja9841761b00005_1","first-page":"1273","volume":"120","author":"George G. N.","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"ja9841761b00006\/ja9841761b00006_1","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1007\/s007750050125","volume":"2","author":"Costa C.","year":"1997","journal-title":"J. Biol. Inorg. Chem."},{"key":"ja9841761b00007\/ja9841761b00007_1","unstructured":"EPR-active molybdopterin radicals (thought to be a MoVItrihydropterin species) have recently been detected in bacterial aldehyde dehydrogenases [Luykx, D. M. A.; Duine, J. A.; de Vries, S.Biochemistry1998,37, 11366\u221211375]. Although such species certainly indicate nonmetal-based redox chemistry, direct involvement of molybdenum ligands is not indicated."},{"key":"ja9841761b00008\/ja9841761b00008_1","unstructured":"X-ray absorption spectroscopic data were collected on SSRL beamline 7-3 as previously described.5,9EXAFS oscillations \u03c7(k) were quantitatively analyzed with EXAFSPAK [http:\/\/ssrl.slac.stanford.edu\/exafspak.html] using ab initio phase and amplitude functions generated withFeffV7.02.10No smoothing, filtering, or related manipulation was performed upon the data. Enzyme samples, at approximately 0.5 mM Mo, were prepared as previously described6in 50 mMN-2-hydroxyethylpiperazine-N\u2018-2-ethanesulfonic acid buffer at pH 7.5 and frozen in 3 \u00d7 10 \u00d7 10 mm Lucite sample cuvettes. The enzyme was reduced with 10 mM sodium dithionite solution in the presence of 40 \u03bcM methyl viologen for 4 min. Dithionite was chosen in preference to formate as reductant because the latter gives rise to a mixture of oxidation states (analysis of EXAFS of mixtures can be problematic). Data were collected at a sample temperature of 10 K and 16 35-min sweeps were averaged for each sample."},{"key":"ja9841761b00009\/ja9841761b00009_1","first-page":"8592","volume":"118","author":"George G. N.","year":"1996","journal-title":"J. Am. Chem. Soc."},{"key":"ja9841761b00010\/ja9841761b00010_1","first-page":"5140","volume":"113","author":"Rehr J. J.","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"ja9841761b00010\/ja9841761b00010_2","first-page":"4156","volume":"44","author":"Mustre de Leon J.","year":"1991","journal-title":"Phys. Rev."},{"key":"ja9841761b00013\/ja9841761b00013_1","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1126\/science.275.5304.1305","volume":"275","author":"Boyington J. C.","year":"1997","journal-title":"Science"},{"key":"ja9841761b00015\/ja9841761b00015_1","first-page":"3923","volume":"3915","author":"Stiefel E. I.","year":"1997","journal-title":"J. Chem. Soc., Dalton Trans."},{"key":"ja9841761b00016\/ja9841761b00016_1","first-page":"7711","volume":"91","author":"Gladyshev V. N.","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"ja9841761b00017\/ja9841761b00017_1","volume":"120","author":"Reports","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"ja9841761b00018\/ja9841761b00018_1","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1021\/bi00410a011","volume":"27","author":"George G. N.","year":"1988","journal-title":"Biochemistry"},{"key":"ja9841761b00019\/ja9841761b00019_1","volume-title":"C. L.","author":"It","year":"1990"}],"container-title":["Journal of the American Chemical Society"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/ja9841761","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,21]],"date-time":"2021-09-21T12:21:19Z","timestamp":1632226879000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/doi\/10.1021\/ja9841761"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,3,1]]},"references-count":18,"journal-issue":{"issue":"11","published-print":{"date-parts":[[1999,3,1]]}},"alternative-id":["10.1021\/ja9841761"],"URL":"https:\/\/doi.org\/10.1021\/ja9841761","relation":{},"ISSN":["0002-7863","1520-5126"],"issn-type":[{"value":"0002-7863","type":"print"},{"value":"1520-5126","type":"electronic"}],"subject":[],"published":{"date-parts":[[1999,3,1]]}}}