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Celia Bonaventura
Researcher at Duke University
Publications - 157
Citations - 7536
Celia Bonaventura is an academic researcher from Duke University. The author has contributed to research in topics: Oxygen binding & Cooperativity. The author has an hindex of 41, co-authored 157 publications receiving 7349 citations. Previous affiliations of Celia Bonaventura include Albert Einstein College of Medicine & College of William & Mary.
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Journal ArticleDOI
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
TL;DR: In this article, the role of S-nitrosohaemoglobin in the transduction of NO-related activities may have therapeutic applications, highlighting newly discovered allosteric and electronic properties of haemoglobin that appear to be involved in the control of blood pressure.
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Fluorescence and oxygen evolution from Chlorella pyrenoidosa.
Celia Bonaventura,Jack Myers +1 more
TL;DR: The model proposes competitive dissipation of absorbed energy by photochemical trapping at reaction centers and by fluorescence and radiationless de-excitation from both the pigment bed and reaction centers of System 2.
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Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
TL;DR: The X‐ray structure of an oxygenated hemocyanin molecule, subunit II of Limulus polyphemus hemocynin, was determined at 2.4 Å resolution and refined to a crystallographic R‐factor of 17.1%.
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Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.
Bart Hazes,Karen A. Magnus,Celia Bonaventura,Joseph Bonaventura,Zbigniev Dauter,Kor H. Kalk,W.G.J. Hol +6 more
TL;DR: The rigid body rotation of the first domain suggests a structural mechanism for the allosteric regulation by chloride ions and probably causes the cooperative transition of the hexamer between low and high oxygen affinity states.
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S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment and lacks O2/NO-linked allosteric function.
Mark T. Gladwin,Xunde Wang,Christopher D. Reiter,Benjamin K. Yang,Esther X. Vivas,Celia Bonaventura,Alan N. Schechter +6 more
TL;DR: Results of these studies show that, within the redox-active erythrocyte environment, the β-globin cysteine 93 is maintained in a reduced state, necessary for normal oxygen affinity, and incapable of oxygen-linked NO storage and delivery.