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Proximal Ligand Motions in H93G Myoglobin
resonance Raman heme myoglobin hemoglobin ligand switch
2016/5/24
Resonance Raman spectroscopy has been used to observe changes in the iron-ligand stretching frequency in photoproduct spectra of the proximal cavity mutant of myoglobin H93G. The measurements compare ...
A Photolysis-Triggered Heme Ligand Switch in H93G Myoglobin
Animals Carbon Monoxide Iron Ferrous Compounds Heme Glycine Myoglobin Ligands Mutagenesis, Insertional Lasers
2016/5/23
Resonance Raman spectroscopy and step-scan Fourier transform infrared (FTIR) spectroscopy have been used to identify the ligation state of ferrous heme iron for the H93G proximal cavity mutant of myog...
The H93G Myoglobin Cavity Mutant as a Versatile Template for Modeling Heme Proteins:Ferrous,Ferric,and Ferryl Mixed-Ligand Complexes with Imidazole in the Cavity
copper(II) azomethine imidate crystal structures
2016/5/23
One of the difficulties in preparing accurate ambient-temperature model complexes for heme proteins, particularly in the ferric state, has been the generation of mixed-ligand adducts: complexes with d...
Assignment of the Heme Axial Ligand(s) for the Ferric Myoglobin (H93G) and Heme Oxygenase (H25A) Cavity Mutants as Oxygen Donors Using Magnetic Circular Dichroism
Alanine Animals Circular Dichroism Electron Transport Glycine Heme Heme Oxygenase (Decyclizing) Heme Oxygenase (Decyclizing) Histidine Humans Hydrogen-Ion Concentration Iron Ligands Mutagenesis, Site-Directed Myoglobin Myoglobin Oxygen Spectrophotometry,Ultraviolet Spectrum Analysis, Raman Titrimetry Whales
2016/5/23
UV-visible absorption and magnetic circular dichroism (MCD) data are reported for the cavity mutants of sperm whale H93G myoglobin and human H25A heme oxygenase in their ferric states at 4 degreesC. D...
Functional Cavities in Proteins:A General Method for Proximal Ligand Substitution in Myoglobin
Functional Cavities Proteins Proximal Ligand Substitution Myoglobin
2016/5/23
Functional Cavities in Proteins:A General Method for Proximal Ligand Substitution in Myoglobin.
Anatomy and Dynamics of a Ligand-Binding Pathway in Myoglobin:The Roles of Residues 45,60,64 and 68
Humans Carbon Monoxide Myoglobin Recombinant Proteins Ligands Spectrum Analysis Protein Binding Kinetics Mutation Thermodynamics
2016/5/23
In order for diatomic ligands to enter and exit myoglobin, there must be substantial displacements of amino acid side chains from their positions in the static X-ray structure. One pathway, involving ...
Discovery of New Ligand Binding Pathways in Myoglobin by Random Mutagenesis
Animals Whales Myoglobin Ligands Genetic Techniques Mutagenesis Binding Sites Amino Acid Sequence Protein Conformation Structure-Activity Relationship
2016/5/23
A random library of single amino acid mutants of myoglobin was generated using a highly efficient, single-base-misincorporation random mutagenesis method to discover new ligand-binding pathways in myo...
Perturbations of the Distal Heme Pocket in Human Myoglobin Mutants Probed by Infrared Spectroscopy of Bound CO:Correlation with Ligand Binding Kinetics
Distal Heme Pocket Human Myoglobin Mutants Probed Infrared Spectroscopy Bound CO:Correlation Ligand Binding Kinetics
2016/5/23
The infrared spectra of CO bound to human myoglobin and myoglobin mutants at positions His-64, Val-68, Asp-60, and Lys-45 on the distal side have been measured between 100 and 300 K. Large differences...
Selective Examination of Heme Protein Azide Ligand-Distal Globin Interactions Vibrational Circular Dichroism
Heme Protein Azide Ligand-Distal Globin Vibrational Circular Dichroism
2016/5/23
Vibrational circular dichroism (VCD) spectra of the antisymmetric stretch of azide ligated to the heme of a series of evolutionarily diverse and site-direct mutant hemoglobins and myoglobins are anoma...
Ligand and Proton Exchange Dynamics in Recombinant Human Myoglobin Mutants
Mb myoglobin n.m.r. nuclear magnetic resonance fwhm full width at half maximum TSP sodium 3-trimethyl silyl propionate DSS 4,4-dimethyl-4-sila pentane-1-sulfonate
2016/5/20
Site-specific mutants of human myoglobin have been prepared in which lysine 45 is replaced by arginine (K45R) and aspartate 60 by glutamate (D60E), in order to examine the influence of these residues ...
