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NO Dioxygenase Activity in Hemoglobins Is Ubiquitous In Vitro, but Limited by Reduction In Vivo
TLDR
It is concluded that any hemoglobin could likely serve this role in the presence of a mechanism for heme iron re-reduction, but that future research to test the role of Hbs in NO scavenging would benefit more from the identification of cognate reductases than from in vitro analysis of NO and O2 binding. Expand
Review: Correlations between oxygen affinity and sequence classifications of plant hemoglobins
TLDR
It is found that sequence classification correlates with distinct extents of hexacoordination with the distal histidine and markedly different overall oxygen affinities and association and dissociation rate constants, which suggest strong selective pressure for the evolution of distinct physiological functions. Expand
Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species.
TLDR
It is demonstrated that hexacoordination could play a much larger role in regulating affinity constants for ligand binding in human neuroglobin and cytoglobin than in the plant hexacoordinate hemoglobins. Expand
Correlations Between Oxygen Affinit y and Sequence Classific ations of Plant Hemoglobins
Smagghe, Benoit J.; Hoy, Julie A.; Percifield, Ryan; Kundu, Suman; Hargrove, Mark S.; Sarath, Gautam; Hilbert, Jean-Louis; Watts, Richard A.; Dennis, Elizabeth S.; Peacock, W. James; DeWilde, Sylvia;Expand
Plant hemoglobins: a molecular fossil record for the evolution of oxygen transport.
TLDR
The crystal structure of the cyanide-bound hexacoordinate hemoglobin from barley is reported, and structural mechanisms for stabilizing the high-energy pentacoordinate heme conformation critical to the evolution of reversible oxygen binding hemoglobins are revealed. Expand
Role of phenylalanine B10 in plant nonsymbiotic hemoglobins.
TLDR
It is shown that Phe at this position is the only amino acid that facilitates stable oxygen binding to the ferrous Hb and the only one that promotes ligand binding in the ferric oxidation states. Expand
Intact αIIbβ3 Integrin Is Extended after Activation as Measured by Solution X-ray Scattering and Electron Microscopy*
TLDR
Small angle x-ray scattering and electron microscopy are used to study detergent-solubilized, intact platelet integrin αIIbβ3 to study the extension and conformational rearrangement upon activation of integrin activation. Expand
Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation
TLDR
It is demonstrated that removal of the His117–heme 2‐vinyl bond increases the affinity constant for intramolecular histidine coordination in the ferric oxidation state, thus presenting greater competition for the ligand binding site and lowering the observed rate and affinity constants for exogenous ligands. Expand
A Primitive Growth Factor, NME7AB, Is Sufficient to Induce Stable Naïve State Human Pluripotency; Reprogramming in This Novel Growth Factor Confers Superior Differentiation
TLDR
A mechanistic model of how human stem cells regulate self-replication is suggested: an early naïve state driven by NME7, which cannot itself limit self‐replication and a later naïve state regulated byNME1, which limits self‐Replication when its multimerization state shifts from the active dimer to the inactive hexamer. Expand
Glutathione-S-transferase is Detected During Somatic Embryogenesis in Chicory
TLDR
The results indicated that GSTs belong to a complex anti-oxidant mechanism within the cell, and also at the cell wall level, and presence in reactivated cell and multicellular embryos is discussed in relation to redox cell status. Expand
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