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The Redox State of the Cell Regulates the Ligand Binding Affinity of Human Neuroglobin and Cytoglobin*
The results suggest a novel mechanism for the regulation of oxygen binding; contact with an appropriate electron donor would provoke the release of oxygen, directly linked to the redox state of the cell. Expand
Sulfide binding is mediated by zinc ions discovered in the crystal structure of a hydrothermal vent tubeworm hemoglobin.
It is demonstrated that zinc ions, not free cysteine residues, bind sulfide in vestimentiferan hemoglobins, challenging the currently accepted paradigm of annelid hemoglobin evolution and adaptation to reducing environments. Expand
Cytoglobin conformations and disulfide bond formation.
The oligomeric state and kinetics of ligand binding were measured for wild-type cytoglobin, which behaves hydrodynamically like a tightly packed globin with a greater flexibility of the N- and C-terminal regions. Expand
Identification of the posttranslational modifications of bovine lens αB‐crystallins by mass spectrometry
Results of this investigation indicate that αB‐crystallin is phosphorylated in vivo at Ser 45, Ser 59, and either Ser 19 or 21, and it appears that there may be two different kinases responsible for their phosphorylation. Expand
Rapid identification of hemoglobin variants by electrospray ionization mass spectrometry.
A rapid approach to variant hemoglobin identification using conventional phenotypic methods combined with electrospray ionization-mass spectrometry (ESI-MS) can now be considered a useful additional tool for reference laboratories. Expand
Mass spectrometric composition and molecular mass of Lumbricus terrestris hemoglobin: a refined model of its quaternary structure.
Sedimentation equilibrium measurements and scanning transmission electron microscopy (STEM) mass mapping of the extracellular, hexagonal bilayer hemoglobin (HBL Hb) of the earthworm LumbricusExpand
Histone‐DNA interactions and their modulation by phosphorylation of ‐Ser‐Pro‐X‐Lys/Arg‐ motifs.
Comparison of some physical and biochemical properties of spermatid and sperm (phosphorylated) chromatin and histones suggests that phosphorylation/dephosphorylation of the N‐terminal (and distal end of the C‐Terminal) tail of H1, and/or the N-terminal Tail of H2B, effectively controls intermolecular interactions between adjacent chromatin filaments, and hence chromatin packing in the sperm nucleus. Expand
Subunit molecular mass assignment of 14,654 Da to the soluble beta-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative
Results point to intramolecular disulfide bonding with a change in protein folding and conformation as the mechanism of oxidative inactivation of the purified bovine lectin. Expand
Cloning, sequencing, and characterization of Escherichia coli thioesterase II.
The gene (tesB) encoding Escherichia coli thioesterase II, a low-abundance enzyme of unknown physiological function which can hydrolyze a broad range of acyl-CoA thioesters, has been localized byExpand