{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T06:18:14Z","timestamp":1780553894710,"version":"3.54.1"},"reference-count":99,"publisher":"American Physiological Society","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Regulatory, Integrative and Comparative Physiology"],"published-print":{"date-parts":[[2013,8,1]]},"abstract":"<jats:p>\n                    In contrast to other vertebrate hemoglobins (Hbs) whose high intrinsic O\n                    <jats:sub>2<\/jats:sub>\n                    affinities are reduced by red cell allosteric effectors (mainly protons, CO\n                    <jats:sub>2<\/jats:sub>\n                    , organic phosphates, and chloride ions), crocodilian Hbs exhibit low sensitivity to organic phosphates and high sensitivity to bicarbonate (HCO\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    ), which is believed to augment Hb-O\n                    <jats:sub>2<\/jats:sub>\n                    unloading during diving and postprandial alkaline tides when blood HCO\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    levels and metabolic rates increase. Examination of \u03b1- and \u03b2-globin amino acid sequences of dwarf caiman ( Paleosuchus palpebrosus) revealed a unique combination of substitutions at key effector binding sites compared with other vertebrate and crocodilian Hbs: \u03b282Lys\u2192Gln, \u03b2143His\u2192Val, and \u03b2146His\u2192Tyr. These substitutions delete positive charges and, along with other distinctive changes in residue charge and polarity, may be expected to disrupt allosteric regulation of Hb-O\n                    <jats:sub>2<\/jats:sub>\n                    affinity. Strikingly, however, P. palpebrosus Hb shows a strong Bohr effect, and marked deoxygenation-linked binding of organic phosphates (ATP and DPG) and CO\n                    <jats:sub>2<\/jats:sub>\n                    as carbamate (contrasting with HCO\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    binding in other crocodilians). Unlike other Hbs, it polymerizes to large complexes in the oxygenated state. The highly unusual properties of P. palpebrosus Hb align with a high content of His residues (potential sites for oxygenation-linked proton binding) and distinctive surface Cys residues that may form intermolecular disulfide bridges upon polymerization. On the basis of its singular properties, P. palpebrosus Hb provides a unique opportunity for studies on structure-function coupling and the evolution of compensatory mechanisms for maintaining tissue O\n                    <jats:sub>2<\/jats:sub>\n                    delivery in Hbs that lack conventional effector-binding residues.\n                  <\/jats:p>","DOI":"10.1152\/ajpregu.00014.2013","type":"journal-article","created":{"date-parts":[[2013,5,30]],"date-time":"2013-05-30T01:03:51Z","timestamp":1369875831000},"page":"R300-R312","source":"Crossref","is-referenced-by-count":37,"title":["Lack of conventional oxygen-linked proton and anion binding sites does not impair allosteric regulation of oxygen binding in dwarf caiman hemoglobin"],"prefix":"10.1152","volume":"305","author":[{"given":"Roy E.","family":"Weber","sequence":"first","affiliation":[{"name":"Zoophysiology, Department of Bioscience, Aarhus University, Aarhus, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angela","family":"Fago","sequence":"additional","affiliation":[{"name":"Zoophysiology, Department of Bioscience, Aarhus University, Aarhus, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans","family":"Malte","sequence":"additional","affiliation":[{"name":"Zoophysiology, Department of Bioscience, Aarhus University, Aarhus, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jay F.","family":"Storz","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, University of Nebraska, Lincoln, Nebraska;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas A.","family":"Gorr","sequence":"additional","affiliation":[{"name":"Institute of Veterinary Physiology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland; and"},{"name":"Center for Pediatrics and Adolescent Medicine, University Medical Center Freiburg, Freiburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00893a021"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1985.tb09032.x"},{"key":"B3","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1016\/S0021-9258(18)97543-5","volume":"240","author":"Antonini E","year":"1965","journal-title":"J Biol Chem"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1021\/bi00708a022"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.1016\/S0305-0491(97)00094-1"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1110\/ps.ps.35702"},{"key":"B7","doi-asserted-by":"publisher","DOI":"10.1016\/0024-3205(69)90455-X"},{"key":"B8","doi-asserted-by":"crossref","first-page":"8429","DOI":"10.1016\/S0021-9258(19)68861-7","volume":"256","author":"Bauer C","year":"1981","journal-title":"J Biol Chem"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1038\/269825a0"},{"key":"B10","doi-asserted-by":"crossref","first-page":"2952","DOI":"10.1016\/S0021-9258(17)40454-6","volume":"252","author":"Bauer C","year":"1977","journal-title":"J Biol Chem"},{"key":"B11","doi-asserted-by":"publisher","DOI":"10.1016\/j.resp.2006.01.002"},{"key":"B12","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(74)90244-7"},{"key":"B13","first-page":"663","volume":"91","author":"Borgese TA","year":"1988","journal-title":"Comp Biochem Physiol"},{"key":"B14","doi-asserted-by":"crossref","first-page":"2361","DOI":"10.1016\/S0021-9258(19)67978-0","volume":"238","author":"Briehl RW","year":"1963","journal-title":"J Biol Chem"},{"key":"B15","doi-asserted-by":"publisher","DOI":"10.1111\/j.1096-3642.2011.00716.x"},{"key":"B16","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(95)00091-1"},{"key":"B17","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1016\/S0021-9258(19)56974-5","volume":"243","author":"Chiancone E","year":"1968","journal-title":"J Biol Chem"},{"key":"B19","doi-asserted-by":"publisher","DOI":"10.1093\/jn\/109.4.538"},{"key":"B20","doi-asserted-by":"publisher","DOI":"10.1016\/0305-0491(83)90418-2"},{"key":"B21","doi-asserted-by":"publisher","DOI":"10.1007\/BF00239974"},{"key":"B22","doi-asserted-by":"publisher","DOI":"10.1016\/S0025-6196(11)63697-5"},{"key":"B23","doi-asserted-by":"publisher","DOI":"10.1016\/0010-406X(70)90662-6"},{"key":"B24","doi-asserted-by":"publisher","DOI":"10.1110\/ps.0234403"},{"key":"B25","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1993.tb18438.x"},{"key":"B26","volume-title":"The Biology of Hagfishes","author":"Fago A","year":"1996"},{"key":"B27","doi-asserted-by":"publisher","DOI":"10.1021\/bi9911379"},{"key":"B28","volume-title":"Atlas of Molecular Structures in Biology. 2. 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