{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T15:29:58Z","timestamp":1778599798778,"version":"3.51.4"},"reference-count":52,"publisher":"American Chemical Society (ACS)","issue":"40","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochemistry"],"published-print":{"date-parts":[[1997,10,1]]},"DOI":"10.1021\/bi971066i","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T05:05:17Z","timestamp":1027659917000},"page":"12120-12137","source":"Crossref","is-referenced-by-count":116,"title":["Probing the Catalytic Mechanism of Sulfite Reductase by X-ray Crystallography:\u2009 Structures of the <i>Escherichia coli<\/i> Hemoprotein in Complex with Substrates, Inhibitors, Intermediates, and Products<sup>,<\/sup>"],"prefix":"10.1021","volume":"36","author":[{"given":"Brian R.","family":"Crane","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lewis M.","family":"Siegel","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth D.","family":"Getzoff","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"316","published-online":{"date-parts":[[1997,10,7]]},"reference":[{"key":"atypb1\/atypb2","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.270.46.27458","volume":"270","author":"Adman E. T.","year":"1995","journal-title":"J. Biol. Chem."},{"key":"atypb3\/atypb4","doi-asserted-by":"crossref","DOI":"10.1021\/ja00279a036","volume":"108","author":"Barley M. H.","year":"1986","journal-title":"J. Am. Chem. Soc."},{"key":"atypb5\/atypb6","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1107\/S0108767378098591","volume":"49","author":"Br\u00fcnger A. T.","year":"1993","journal-title":"Acta Crystallogr."},{"key":"atypb7\/atypb8","volume-title":"Science 235, 458\u2212460","author":"Br\u00fcnger A. T.","year":"1987"},{"key":"atypb9\/atypb10","volume":"102","author":"Chang C. K.","year":"1980","journal-title":"J. Am. Chem. Soc."},{"key":"atypb11\/atypb12","volume-title":"Advanced Inorganic Chemistry","author":"Cotton F. A.","year":"1988","edition":"5"},{"key":"atypb13\/atypb14","volume-title":"Curr. Opin. Struct. Biol. 6, 744\u2212756","author":"Crane B. R.","year":"1996"},{"key":"atypb15\/atypb16","first-page":"40","volume":"53","author":"Crane B. R.","year":"1997","journal-title":"Acta Crystallogr."},{"key":"atypb17\/atypb18","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1126\/science.270.5233.59","volume":"270","author":"Crane B. R.","year":"1995","journal-title":"Science"},{"key":"atypb19\/atypb20","volume-title":"Biochemistry 36, 12101\u221212119","author":"Crane B. R.","year":"1997"},{"key":"atypb21\/atypb22","volume-title":"Science 240, 1308\u22121319","author":"Dawson J. H.","year":"1988"},{"key":"atypb23\/atypb24","volume-title":"Biochemistry 27, 2126\u22122132","author":"Day E. P.","year":"1988"},{"key":"atypb25\/atypb26","volume-title":"Top. Stereochem. 12, 155\u2212215","author":"Feltham R. D.","year":"1981"},{"key":"atypb27\/atypb28","volume":"105","author":"Fujita E.","year":"1983","journal-title":"J. Am. Chem. Soc."},{"key":"atypb29\/atypb30","volume-title":"Science 275, 1471\u22121475","author":"Genick U. K.","year":"1997"},{"key":"atypb31\/atypb32","volume":"12","author":"Ginn V.","year":"1993","journal-title":"J. Chem. Soc., Dalton Trans."},{"key":"atypb33\/atypb34","volume-title":"Biochemistry 28, 5477\u22125485","author":"Han S.","year":"1989"},{"key":"atypb35\/atypb36","doi-asserted-by":"crossref","DOI":"10.1107\/S0108767392006044","volume":"48","author":"Hodel A.","year":"1992","journal-title":"Acta Crystallogr."},{"key":"atypb37\/atypb38","volume-title":"Biochemistry 21, 3538\u22123547","author":"Janick P.","year":"1982"},{"key":"atypb39\/atypb40","volume-title":"Biochemistry 22, 504\u2212515","author":"Janick P.","year":"1983"},{"key":"atypb41\/atypb42","volume-title":"Biochemistry 22, 396\u2212408","author":"Janick P. A.","year":"1983"},{"key":"atypb43\/atypb44","volume":"21","author":"Kabsch W. J.","year":"1988","journal-title":"J. Appl. Crystallogr."},{"key":"atypb45\/atypb46","volume-title":"Biochemistry 32, 2853\u22122867","author":"Kaufman J.","year":"1993"},{"key":"atypb47\/atypb48","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1006\/bbrc.1995.1310","volume":"208","author":"Kimata Y.","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"atypb49\/atypb50","volume-title":"Biochemistry 21, 2892\u22122904","author":"Krueger R. J.","year":"1982"},{"key":"atypb51\/atypb52","volume":"115","author":"Lui S. M.","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"atypb53\/atypb54","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/0263-7855(92)80022-6","volume":"10","author":"McRee D. E.","year":"1992","journal-title":"J. Mol. Graphics"},{"key":"atypb55\/atypb56","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(19)42924-4","volume":"249","author":"Murphy M. J.","year":"1974","journal-title":"J. Biol. Chem."},{"key":"atypb57\/atypb58","volume-title":"Adv. Inorg. Chem. 38, 423\u2212469","author":"Noodleman L.","year":"1992"},{"key":"atypb59\/atypb60","first-page":"62","volume-title":"L., Isaacs, N., & Bailey","author":"Otwinowski Z.","year":"1993"},{"key":"atypb61\/atypb62","volume-title":"II (Lever, A. B. P., & Gray","author":"Palmer G.","year":"1983"},{"key":"atypb63\/atypb64","first-page":"132","volume-title":"J. A., & Ferguson","author":"Peck H. D., Jr.","year":"1988"},{"key":"atypb65\/atypb66","volume-title":"G. L., & Marzilli","author":"Poulos T. L.","year":"1988"},{"key":"atypb67\/atypb68","volume":"42","author":"Read R. J.","year":"1988","journal-title":"Acta Crystallogr."},{"key":"atypb69\/atypb70","first-page":"140","volume-title":"A. B. P., & Gray","author":"Scheidt W. M.","year":"1983"},{"key":"atypb71\/atypb72","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1021\/ja00834a006","volume":"97","author":"Scheidt W. R.","year":"1975","journal-title":"J. Am. Chem. Soc."},{"key":"atypb73\/atypb74","volume":"98","author":"Scheidt W. R.","year":"1976","journal-title":"J. Am. Chem. Soc."},{"key":"atypb75\/atypb76","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(19)42921-9","volume":"249","author":"Siegel L. M.","year":"1974","journal-title":"J. Biol. Chem."},{"key":"atypb77\/atypb78","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(19)42921-9","volume":"249","author":"Siegel L. M.","year":"1974","journal-title":"J. Biol. Chem."},{"key":"atypb79\/atypb80","volume":"248","author":"Siegel L. M.","year":"1973","journal-title":"J. Biol. Chem."},{"key":"atypb81\/atypb82","volume":"257","author":"Siegel L. M.","year":"1982","journal-title":"J. Biol. Chem."},{"key":"atypb83\/atypb84","doi-asserted-by":"crossref","DOI":"10.1021\/cr9500500","volume":"96","author":"Sono M.","year":"1996","journal-title":"Chem. Rev."},{"key":"atypb85\/atypb86","volume-title":"Biochemistry 30, 8910\u22128917","author":"Tan J.","year":"1991"},{"key":"atypb87\/atypb88","first-page":"42","volume":"9","author":"Upson C.","year":"1989","journal-title":"IEEE Comp. G."},{"key":"atypb89\/atypb90","volume":"252","author":"Vega J. M.","year":"1977","journal-title":"J. Biol. Chem."},{"key":"atypb91\/atypb92","volume-title":"ACS Symp. Ser. 612, 280\u2212292","author":"Wairavamurthy M.","year":"1995"},{"key":"atypb93\/atypb94","volume-title":"Biochemistry 27, 2790\u22122800","author":"Young L. J.","year":"1988"},{"key":"atypb95\/atypb96","volume-title":"Biochemistry 27, 4991\u22124999","author":"Young L. J.","year":"1988"},{"key":"bi971066ib00001\/bi971066ib00001_1","volume-title":"ethylenediaminetetraacetic acid","author":"Abbreviations HEPES"},{"key":"bi971066ib00003\/bi971066ib00003_1","unstructured":"AlthoughR-Free (Brunger, 1993) was evaluated for the initial positional refinements of HP\u2212SO3, HP\u2212PO4Cr(II), and HP\u2212CO, all of the diffraction data were included in the high-resolution refinements so that the maximum amount of diffraction information would contribute to defining the cofactor and ligand geometry. Because the apparent structural changes in all complexes were localized to the active center and were relatively small compared to the overall structural consistency of the SiRHP protein moiety, phase bias introduced by the ligand-free oxidized SiRHP model was not a grave concern.R-Free was not a sensitive enough criterion to differentiate alternative bonding geometries of phosphate or sulfite to the siroheme."},{"key":"bi971066ib00007\/bi971066ib00007_1","unstructured":"This movement is not reflected in the unrestrained refined geometrical parameters of Table 2 which show equal distances between the bridging thiolate and siroheme iron for HP\u2212CO and HP\u2212CN; however, a small difference is beyond the sensitivity of the refinement, given the resolution of the diffraction data sets. It is also possible that traces of the HP\u2212PO4Cr(II) structure remain in the HP\u2212CO simulated data (see Experimental Procedures) that slightly skew the iron position in HP\u2212CO toward a domed conformation."},{"key":"bi971066ib00009\/bi971066ib00009_1","unstructured":"Although comparison of catalytic rates between the SiR holoenzyme with NADPH as an electron donor and the isolated hemoprotein with nonnatural electron donors suggests that electron transfer from NADPH to the coupled cofactors is rate-limiting in the holoenzyme (Siegelet al., 1974; Siegel & Davis, 1974), different rates for for the reduction of HSO3-, NO2-, and NH2OH by the SiR holoenzyme indicate that the rate of catalysis is not completely independent of substrate (Siegelet al., 1974)."}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/bi971066i","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,16]],"date-time":"2021-10-16T22:42:34Z","timestamp":1634424154000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/doi\/10.1021\/bi971066i"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,10,1]]},"references-count":52,"journal-issue":{"issue":"40","published-print":{"date-parts":[[1997,10,1]]}},"alternative-id":["10.1021\/bi971066i"],"URL":"https:\/\/doi.org\/10.1021\/bi971066i","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,10,1]]}}}