{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T08:06:42Z","timestamp":1792570002661,"version":"4.5.0"},"reference-count":27,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2002,6,21]],"date-time":"2002-06-21T00:00:00Z","timestamp":1024617600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2002,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Light\u2010absorption spectra and afferent chemoreceptor discharge were simultaneously recorded on superfused rat carotid bodies (CBs) under the influence of cytochrome a3\u2010CuB ligands (O2, CN\n                    <jats:sup>\u2013<\/jats:sup>\n                    , CO) in order to identify the primary mitochondrial cytochrome c oxidase (CCO) oxygen sensor. Spectra could be described on the basis of weighted light\u2010absorption spectra of cytochrome b558 of the NAD(P)H oxidase and mitochondrial cytochromes b and c, CCO, cytochrome a3, and an unusual cytochrome a peaking at 592 nm. Discharge signals were deconvoluted into phasic and tonic activity for comparing different CB responses. The spectral weight of cytochrome a592 decreased significantly starting at high PO2 (100 mm Hg) and low sodium cyanide (CN\n                    <jats:sup>\u2013<\/jats:sup>\n                    , 10 \u03bcM) accompanied by increasing phasic peak discharge. Combined CO\u2010hypoxia or CO\u2010CN\n                    <jats:sup>\u2013<\/jats:sup>\n                    application inhibited photolysis of CO\u2010stimulated chemoreceptor discharge, revealing photometrically cytochrome a592 as central in oxygen sensing. Control spectra in tissue from sympathetic and nodose ganglia did not show any cytochrome a592 contribution. According to these results, cytochrome a592 is assumed as a unique component of CB CCO, revealing in contrast to other cytochromes an apparent low PO2 and high CN\n                    <jats:sup>\u2013<\/jats:sup>\n                    affinity, probably due to a shortcut of electron flow within CCO between CuA and cytochrome a3\u2010CuB.\n                  <\/jats:p>","DOI":"10.1096\/fj.02-0166fje","type":"journal-article","created":{"date-parts":[[2002,9,30]],"date-time":"2002-09-30T13:43:21Z","timestamp":1033393401000},"page":"1277-1279","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":38,"title":["Unusual cytochrome a\n                    <sub>592<\/sub>\n                    with low PO\n                    <sub>2<\/sub>\n                    affinity correlates as putative oxygen sensor with rat carotid body chemoreceptor discharge"],"prefix":"10.1096","volume":"16","author":[{"given":"Tino","family":"Streller","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Physiologie der Universit\u00e4t Rostock  Gertrudenstrasse 9 18057 Rostock Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Huckstorf","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physiologie der Universit\u00e4t Rostock  Gertrudenstrasse 9 18057 Rostock Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christfried","family":"Pfeiffer","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physiologie der Universit\u00e4t Rostock  Gertrudenstrasse 9 18057 Rostock Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helmut","family":"Acker","sequence":"additional","affiliation":[{"name":"Max Planck Institut f\u00fcr Molekulare Physiologie  Otto\u2010Hahn\u2010Strasse 11 44227 Dortmund Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2002,6,21]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.1996.76.3.839"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.physiol.63.1.259"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1177\/002215549704500707"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1152\/jn.1972.35.4.405"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(94)00887-6"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj2720743"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1152\/jappl.2000.88.6.2287"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1469-7793.2000.00135.x"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0034-5687(99)00014-6"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.16.9427"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(96)00014-X"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biophys.27.1.329"},{"key":"e_1_2_6_14_1","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.274.53.37974","article-title":"Mutation of Arg\u201054 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase","volume":"274","author":"Kannt A.","year":"1999","journal-title":"JBC"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0034-5687(01)00310-3"},{"key":"e_1_2_6_16_1","first-page":"284","article-title":"The pathway of CO binding to cytochrome c oxidase","volume":"354","author":"Hill B. 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