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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.
Disentangling electrospray spectra with maximum entropy
Sulfide binding is mediated by zinc ions discovered in the crystal structure of a hydrothermal vent tubeworm hemoglobin.
- J. Flores, C. Fisher, W. Royer
- BiologyProceedings of the National Academy of Sciences…
- 22 February 2005
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.
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.
Identification of the posttranslational modifications of bovine lens αB‐crystallins by mass spectrometry
- Jean B. Smith, Yiping Sun, David L. Smith, B. Green
- Chemistry, BiologyProtein science : a publication of the Protein…
- 1 May 1992
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.
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.
Cloning, sequencing, and characterization of Escherichia coli thioesterase II.
Elucidation of the primary structures of proteins by mass spectrometry.
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 Lumbricus…
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.