{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T09:13:37Z","timestamp":1791191617404,"version":"4.1.0"},"reference-count":39,"publisher":"National Academy of Sciences","issue":"18","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2001,8,28]]},"abstract":"<jats:p>\n                    We have previously reported that bacterial flavohemoglobin (HMP) catalyzes both a rapid reaction of heme-bound O\n                    <jats:sub>2<\/jats:sub>\n                    with nitric oxide (NO) to form nitrate [HMP-Fe(II)O\n                    <jats:sub>2<\/jats:sub>\n                    + NO \u2192 HMP-Fe(III) + NO\n                    <jats:inline-formula>\n                      <jats:tex-math notation=\"LaTeX\">\\documentclass[12pt]{minimal}\n\\usepackage{amsmath}\n\\usepackage{wasysym} \n\\usepackage{amsfonts} \n\\usepackage{amssymb} \n\\usepackage{amsbsy}\n\\usepackage{mathrsfs}\n\\setlength{\\oddsidemargin}{-69pt}\n\\begin{document}\n\\begin{equation*}{\\mathrm{_{3}^{-}}}\\end{equation*}\\end{document}<\/jats:tex-math>\n                    <\/jats:inline-formula>\n                    ] and, under anaerobic conditions, a slower reduction of heme-bound NO to an NO\n                    <jats:sup>\u2212<\/jats:sup>\n                    equivalent (followed by the formation of N\n                    <jats:sub>2<\/jats:sub>\n                    O), thereby protecting against nitrosative stress under both aerobic and anaerobic conditions, and rationalizing our finding that NO is rapidly consumed across a wide range of O\n                    <jats:sub>2<\/jats:sub>\n                    concentrations. It has been alternatively suggested that HMP activity is inhibited at low pO\n                    <jats:sub>2<\/jats:sub>\n                    because the enzyme is then in the relatively inactive nitrosyl form [\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>off<\/jats:sub>\n                    \/\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>on<\/jats:sub>\n                    for NO (0.000008 \u03bcM) \u226a\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>off<\/jats:sub>\n                    \/\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>on<\/jats:sub>\n                    for O\n                    <jats:sub>2<\/jats:sub>\n                    (0.012 \u03bcM) and\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>M<\/jats:sub>\n                    for O\n                    <jats:sub>2<\/jats:sub>\n                    = 30\u2013100 \u03bcM]. To resolve this discrepancy, we have directly measured heme-ligand turnover and NADH consumption under various O\n                    <jats:sub>2<\/jats:sub>\n                    \/NO concentrations. We find that, at biologically relevant O\n                    <jats:sub>2<\/jats:sub>\n                    concentrations, HMP preferentially binds NO (not O\n                    <jats:sub>2<\/jats:sub>\n                    ), which it then reacts with oxygen to form nitrate (in essence NO\n                    <jats:sup>\u2212<\/jats:sup>\n                    + O\n                    <jats:sub>2<\/jats:sub>\n                    \u2192 NO\n                    <jats:inline-formula>\n                      <jats:tex-math notation=\"LaTeX\">\\documentclass[12pt]{minimal}\n\\usepackage{amsmath}\n\\usepackage{wasysym} \n\\usepackage{amsfonts} \n\\usepackage{amssymb} \n\\usepackage{amsbsy}\n\\usepackage{mathrsfs}\n\\setlength{\\oddsidemargin}{-69pt}\n\\begin{document}\n\\begin{equation*}{\\mathrm{_{3}^{-}}}\\end{equation*}\\end{document}<\/jats:tex-math>\n                    <\/jats:inline-formula>\n                    ). During steady-state turnover, the enzyme can be found in the ferric (FeIII) state. The formation of a heme-bound nitroxyl equivalent and its subsequent oxidation is a novel enzymatic function, and one that dominates the oxygenase activity under biologically relevant conditions. These data unify the mechanism of HMP\/NO interaction with those recently described for the nematode Ascaris and mammalian hemoglobins, and more generally suggest that the peroxidase (FeIII)-like properties of globins have evolved for handling of NO.\n                  <\/jats:p>","DOI":"10.1073\/pnas.181199698","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:45:09Z","timestamp":1027680309000},"page":"10108-10112","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":141,"title":["Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen"],"prefix":"10.1073","volume":"98","author":[{"given":"Alfred","family":"Hausladen","sequence":"first","affiliation":[{"name":"Departments of Medicine and Biochemistry and Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Gow","sequence":"additional","affiliation":[{"name":"Departments of Medicine and Biochemistry and Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan S.","family":"Stamler","sequence":"additional","affiliation":[{"name":"Departments of Medicine and Biochemistry and Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2001,8,21]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1038\/202083b0"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.67.4.1846"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi980941c"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0162-0134(00)80291-3"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi960442g"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/380221a0"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.16.9027"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M000532200"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.090083597"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1038\/34402"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.20.12543"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.24.14100"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.18.10378"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.2.748"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(99)00157-X"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.275.17.12581"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3530207"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(96)00208-9"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M004141200"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.041481598"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1995.tb00297.x"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M009280200"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1038\/46822"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.14.6399"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.3181\/00379727-147-38275"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9610(05)80576-8"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1164\/ajrccm.159.6.9801124"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.11.5015"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.12.5675"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.molbev.a025592"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.286.5444.1571"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1038\/32831"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.276.5313.734"},{"key":"e_1_3_3_34_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.11536547"},{"key":"e_1_3_3_35_2","doi-asserted-by":"publisher","DOI":"10.1242\/jeb.201.8.1099"},{"key":"e_1_3_3_36_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.203.4384.1002"},{"key":"e_1_3_3_37_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01808213"},{"key":"e_1_3_3_38_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1469-8137.1998.00168.x"},{"key":"e_1_3_3_39_2","doi-asserted-by":"publisher","DOI":"10.1128\/mmbr.61.4.533-616.1997"}],"container-title":["Proceedings 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