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S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
These findings highlight newly discovered allosteric and electronic properties of haemoglobin that appear to be involved in the control of blood pressure and which may facilitate efficient delivery of oxygen to tissues.
Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation
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.
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
- K. Magnus, B. Hazes, H. Ton-that, C. Bonaventura, J. Bonaventura, W. Hol
- ChemistryProteins: Structure, Function, and Bioinformatics
- 1 August 1994
The X‐ray structure of an oxygenated hemocyanin molecule, subunit II of Limulus polyphemus hemocyanin, was determined at 2.4 Å resolution and refined to a crystallographic R‐factor of 17.1%. The…
Allosteric modulation of Callinectes sapidus hemocyanin by binding of L-lactate.
The results are consistent with the role of L-lactate as a specific allosteric effector of Callinectes hemocyanin that acts by preferential binding to a stereospecific site of the oxy hemOCyanin.
S-Nitrosohemoglobin Is Unstable in the Reductive Erythrocyte Environment and Lacks O2/NO-linked Allosteric Function*
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.
New insights into the proton-dependent oxygen affinity of Root effect haemoglobins.
The available evidence supports the concept that in both Bohr effect and Root effect Hbs a large steric component acts in addition to quaternary shifts between R and T conformations to regulate ligand affinity, and moderate these steric effects within both R- and T-state conformations.
Structural basis for the Root effect in haemoglobin
- S. Mylvaganam, C. Bonaventura, J. Bonaventura, E. Getzoff
- BiologyNature Structural Biology
- 1 March 1996
Surprisingly, a set of residues specific to Root effect haemoglobins recruit additional residues, conserved among most haemglobins, to produce the Root effect.
Hemoglobins of two terebellid polychaetes: Enoplobranchus sanguineus and Amphitrite ornata.
Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers.