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| CELIA J BONAVENTURASummaryAffiliation: Duke University Medical Center Country: USA Publications
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Publications
Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxideC Bonaventura
Marine Freshwater Biomedical Center, Duke University Marine Laboratory, Beaufort, North Carolina 28516, USA
J Biol Chem 274:5499-507. 1999..The beta hemes in Cu(II)-metHb are reduced under CO at rates close to those observed for cytochrome c oxidase, where heme and copper are present together in the oxygen-binding site and where internal electron transfer also occurs...- Effects of S-nitrosation on oxygen binding by normal and sickle cell hemoglobinC Bonaventura
Duke University Marine Biomedical Center, Nicholas School of the Environment Marine Laboratory, Beaufort, North Carolina 28516, USA
J Biol Chem 274:24742-8. 1999..The increased oxygen affinity and R-state character that result from S-nitrosation of Hb S would be expected to decrease its polymerization and thereby lessen the associated symptoms of sickle cell disease... - Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell diseaseCelia Bonaventura
Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, Beaufort, NC 28516, USA
Biophys Chem 98:165-81. 2002..S-nitrosation is thus shown to have an effect similar to that reported for other SH-group modifications of Hb S, in which R-state stabilization opposes Hb S aggregation... - Critical redox and allosteric aspects of nitric oxide interactions with hemoglobinCelia Bonaventura
Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, Beaufort, NC 28516, USA
Antioxid Redox Signal 6:979-91. 2004..In spite of low levels of NO-Hb and SNO-Hb found in vivo, recent findings do not rule out participation of NO-Hb or SNO-Hb in NO-dependent signaling reactions... - Overproduction of alpha chains provides a proton-insensitive component to the bluefish hemoglobin systemCelia Bonaventura
Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, Beaufort, North Carolina 28516, USA
J Biol Chem 280:40509-14. 2005..This is the first reported case of a thalassemic condition that is maintained in a species as an adaptive advantage... - Allosteric effects on oxidative and nitrosative reactions of cell-free hemoglobinsCelia Bonaventura
Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, Beaufort, North Carolina 28516, USA
IUBMB Life 59:498-505. 2007..These redox reactions can drive formation of SNO-Hb and other reactive species and are of significance for the use of cell-free Hbs in vivo... - Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitriteCelia Bonaventura
Nicholas School of the Environment, Duke University Marine Laboratory, Beaufort, NC 28516, USA
Biochim Biophys Acta 1804:1988-95. 2010..These results provide a dramatic illustration of how evolution of active sites with varied heme accessibility can moderate the rates of inner-sphere oxidative reactions of Hb and other heme proteins... - Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobinsCelia Bonaventura
Duke University Marine Laboratory, Beaufort, NC 28516, USA
Biochim Biophys Acta 1814:1261-8. 2011..Evolution of Hb sequences that result in proton-linked steric barriers to heme oxygenation could provide a general mechanism to account for the appearance of the Root effect in the structurally diverse Hbs of many species...