Opossum hemoglobin. The amino acid sequences of the alpha and beta chains.

  title={Opossum hemoglobin. The amino acid sequences of the alpha and beta chains.},
  author={Peter Stenzel and Bernadine Brimhall and R. T. Jones and John A. Black and Anne McLachlan and D R Gibson},
  journal={The Journal of biological chemistry},
  volume={254 6},
An exceptional amino acid replacement on the distal side of the iron atom in proboscidean myoglobin
Comparative sequence data of paenungulate myoglobins suggest that the His → Gln mutation probably occurred in an ancestor of Elephantinae.
Nitrosyl Myoglobins and Their Nitrite Precursors: Crystal Structural and Quantum Mechanics and Molecular Mechanics Theoretical Investigations of Preferred Fe -NO Ligand Orientations in Myoglobin Distal Pockets.
The interactions of nitrite with wt sperm whale (sw) MbIII and its H64A, H64Q, and V68A/I107Y mutants are reported and their FeNO orientations vary with distal pocket identity, with the FeNO moieties pointing toward the hydrophobic interiors when the His64 residue is present but toward the Hydrophilic exterior when this His 64 residue is absent.
Distribution, adaptation and physiological meaning of thiols from vertebrate hemoglobins.
Hemoglobins, XLVIIII
The genetic codes of Myxine and Lampetra hemoglobins show 117 differences, in spite of many morphological resemblances between hagfish and lamprey, and their primary hemoglobin structures show differences substantial enough to bo compatible with the divergence of the two families some 400–500 million years ago.
Solution and Crystal Structures of a Sperm Whale Myoglobin Triple Mutant That Mimics the Sulfide-binding Hemoglobin fromLucina pectinata *
The bivalve mollusc Lucina pectinataharbors sulfide-oxidizing chemoautotrophic bacteria and expresses a monomeric hemoglobin I, HbI, with normal O2, but extraordinarily high sulfide affinity has revealed an active site with three residues not commonly found in vertebrate globins.
Effect of the distal residues on the vibrational modes of the Fe-CO bond in hemoglobin studied by protein engineering.
Using an Escherichia coli gene expression system, human hemoglobin mutants are engineered having the distal histidine and valine residues replaced by other amino acids, finding that the steric bulk of thedistal residues is not the primary determinant of the Fe-CO ligand vibrational frequencies.
Infrared spectra of carbonyl hemoglobins: characterization of dynamic heme pocket conformers.
The infrared spectra for carbon monoxide complexed to hemoglobins were examined in the C-O stretch region and provide qualitative and quantitative information on the structural dynamics, stability, and ligand binding properties of hemoglOBins.
Globin Macromolecular Sequences in Marsupials and Monotremes
It is argued that continuing studies of marsupial and monotreme globins, particularly molecular studies on gene organisation and regulation, are likely to contribute significantly to the understanding of gene and organismal evolution.