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Proximal Ligand Motions in H93G Myoglobin
resonance Raman heme myoglobin hemoglobin ligand switch
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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 ...
FTIR and Resonance Raman Studies of Nitric Oxide Binding to H93G Cavity Mutants of Myoglobin
Animals Nitric Oxide Imidazoles Myoglobin Enzyme Inhibitors Free Radical Scavengers Spectroscopy, Fourier Transform Infrared Spectrum Analysis, Raman Binding Sites Molecular Structure
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2016/5/23
Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a five- or six-coordinate Fe-NO complex. The H93G mutation eliminates the covalent attachment between the protein and ...
19F NMR of Trifluoroacetyl-Labeled Cysteine Mutants of Myoglobin:Structural Probes of Nitric Oxide Bound to the H93G Cavity Mutant
19F NMR Trifluoroacetyl Cysteine Mutants Myoglobin Nitric Oxide H93G Cavity Mutant
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2016/5/23
Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a 5- or 6-coordinate Fe--NO heme complex. The H93G mutation replaces the proximal histidine of Mb with glycine, allowi...
A Photolysis-Triggered Heme Ligand Switch in H93G Myoglobin
Animals Carbon Monoxide Iron Ferrous Compounds Heme Glycine Myoglobin Ligands Mutagenesis, Insertional Lasers
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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
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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...
Resonance Raman Studies of Heme Axial Ligation in H93G Myoglobin
chemical vapor deposition diamond electron microscopy epitaxy iridium surface structure,morphology,roughness,and topography
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2016/5/23
The resonant Raman active mode identified in numerous studies as the heme iron−histidine stretch has been systematically investigated in the Raman spectrum of 15 exogenous ligands to the heme ir...
The Role of the Distal and Proximal Protein Environments in Controlling the Ferric Spin State and in Stabilizing Thiolate Ligation in Heme Systems:Thiolate Adducts of the Myoglobin H93G Cavity Mutant
salicylic alcohols hydrogen bonds quantum chemistry
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2016/5/23
Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by ...
Hydrogen Bonding Modulates Binding of Exogenous Ligands in a Myoglobin Proximal Cavity Mutant
Alanine Amino Acid Substitution Animals Binding Sites Glycine Histidine Hydrogen Bonding Imidazoles Ligands Macromolecular Substances Metmyoglobin Models, Chemical Mutagenesis, Insertional Myoglobin Nitric Oxide Nuclear Magnetic Resonance,Biomolecular Protons Serine Threonine Whales
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2016/5/23
In the sperm whale myoglobin mutant H93G, the proximal histidine is replaced by glycine, leaving a cavity in which exogenous imidazole can bind and ligate the heme iron (Barrick, D. (1994) Biochemistr...
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
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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...
Dynamics of Myoglobin-CO with the Proximal Histidine Removed:Vibrational Echo Experiments
Myoglobin-CO Proximal Histidine Removed Vibrational Echo Experiments
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2016/5/23
Picosecond infrared vibrational echo measurements from 60 to 300 K on CO bound to the active site of a mutant myoglobin, H93G(N-MeIm), are presented and compared to measurements on native myoglobin an...
On the Origin of Heme Absorption Band Shifts and Associated Protein Structural Relaxation in Myoglobin Following Flash Photolysis
transhydrogenase NAD NADP Escherichia coli proton pump metal ion
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2016/5/23
The role of the protein structural change monitored by absorption band shifts following flash photolysis of CO from myoglobin is discussed in terms of structure-function relationships. Evidence is pre...
Trans Effects in Nitric Oxide Binding to Myoglobin Cavity Mutant H93G
biology and medicine, basic studies nitric oxide biochemistry heme histidine imidazoles ligands mutants myoglobin proteins
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2016/5/23
When nitric oxide (NO) binds to heme proteins, it exerts a repulsive trans effect on the proximal ligand, resulting in weakening or rupture of the proximal ligand-iron bond. The general question of wh...
Modulation of Protein Function by Exogenous Ligands in Protein Cavities:CO Binding to a Myoglobin Cavity Mutant Containing Unnatural Proximal Ligands
Animals Binding Sites Carbon Monoxide Cloning, Molecular Escherichia coli Heme Kinetics Ligands Magnetic Resonance Spectroscopy Mutagenesis, Site-Directed Myoglobin Myoglobin Point Mutation Protein Conformation ecombinant Proteins Recombinant Proteins Spectroscopy,Fourier Transform Infrared Valine Whales
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2016/5/23
A variety of heterocyclic ligands can be exchanged into the proximal cavity of sperm whale myoglobin mutant H93G, providing a simple method for introduction of the equivalent of unnatural amino acid s...
Functional Aspects of Ultra-rapid Heme Doming in Hemoglobin,Myoglobin,and the Myoglobin Mutant H93G
Animals Carboxyhemoglobin Carboxyhemoglobin Heme Hemoglobins Hemoglobins Horses Kinetics Myoglobin Myoglobin Myoglobin Point Mutation Spectrum Analysis, Raman Time Factors Whales
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2016/5/23
Heme iron out-of-plane displacement following ligand dissociation in hemoglobin, myoglobin, and the proximal cavity mutant H93G is shown to be as rapid as the heme iron out-of-plane vibrational period...
Casting a Cold Eye over Myoglobin
Cold Temperature Crystallography,X-Ray Myoglobin Myoglobin Photolysis Protein Conformation
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2016/5/23
Structural studies of carbonmonoxy myoglobin photolyzed at ultra-low temperatures have allowed the visualization of an otherwise elusive binding intermediate.