A comparison of the geminate recombination kinetics of several monomeric heme proteins.
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TLDR
The differences between the CO-, O2-, and NO-binding parameters for R and T state hemoglobin appear to be due to a decrease in the geminate reactivity of the heme iron atom, with little or no change in the accessibility of the distal pocket.About:
This article is published in Journal of Biological Chemistry.The article was published on 1988-02-05 and is currently open access. It has received 59 citations till now. The article focuses on the topics: Leghemoglobin & Myoglobin.read more
Citations
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Journal ArticleDOI
The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin.
Ronald J. Rohlfs,Antony J. Mathews,Theodore E. Carver,John S. Olson,Barry A. Springer,Karen D. Egeberg,Stephen G. Sligar +6 more
TL;DR: The measured association rate constants suggest that a major kinetic barrier for O2 and CO binding to native myoglobin may involve disruption of polar interactions between His64 and water molecules found in the distal pocket of deoxymyoglobin.
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Imaging the migration pathways for O2, CO, NO, and Xe inside myoglobin
TL;DR: This work presents a complete map of all the gas migration pathways inside Mb for small gas ligands (O2, NO, CO, and Xe), and introduces a computational approach for studying gas migration, which is called implicit ligand sampling.
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A hemoglobin from plants homologous to truncated hemoglobins of microorganisms
R. A. Watts,Peter Hunt,A. N. Hvitved,Mark S. Hargrove,William James Peacock,Elizabeth S. Dennis +5 more
TL;DR: The analysis of the sequence, ligand interactions, and expression profile of GLB3 indicates that this protein has unique biochemical properties, evolutionary history, and, most likely, a function distinct from those of other plant Hbs.
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Chemical nature of nitric oxide storage forms in rat vascular tissue
TL;DR: In this article, aortic tissue homogenates were analyzed by using chemiluminescence and ion-chromatography-based techniques that allow trace-level quantification of NO-related compounds in complex biological matrices.
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Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands.
D W Kraus,Jonathan B. Wittenberg +1 more
TL;DR: Three hemoglobins have been isolated from the symbiont-harboring gill of the bivalve mollusc Lucina pectinata and it is inferred that Hb I may facilitate delivery of hydrogen sulfide to the chemoautotrophic bacterial Symbiont and Hb II and HB III may facilitate Delivery of oxygen.
References
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Dynamics of ligand binding to myoglobin
TL;DR: The nonexponential rebinding observed at low temperatures and in solid samples implies that the innermost barrier has a spectrum of activation energies, similar to how myoglobin achieves specificity and order.
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Leghemoglobin and rhizobium respiration
TL;DR: The author revealed that Rhizobium Nitrogen Fixation Without Leghemoglobin could have been caused by either Nitrogenase Location and Oxygen Lability or Periplasmic Location of Bacteroid Oxidases.
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Cooperativity in the dissociation of nitric oxide from hemoglobin.
E G Moore,Q H Gibson +1 more
TL;DR: The results show that if the equilibrium binding curve for NO could be determined experimentally, it would show cooperativity with Hill's n at 50% saturation of about 1.6.
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Conformation, co-operativity and ligand binding in human hemoglobin.
Robert Cassoly,Quentin H. Gibson +1 more
TL;DR: In spite of the absence of co-operativity, the normal T → R transition occurs on nitric oxide binding, as demonstrated by the release of 8-hydroxy-1,3,6-pyrene trisulfonate, and the R-state shows the normal enhancement of reactivity towards carbon monoxide as compared with the T-state.
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Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin.
C A Sawicki,Q H Gibson +1 more
TL;DR: Kinetic results obtained below pH 8 are found to be inconsistent with a two-state model, and it appears that binding of inositol hexaphosphate produces a new rapidly reacting quaternary conformation of HbCO.