搜索结果: 1-15 共查到“多肽与蛋白质生物化学 Myoglobin”相关记录19条 . 查询时间(0.066 秒)
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 ...
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
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
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...
Dynamics of Myoglobin-CO with the Proximal Histidine Removed:Vibrational Echo Experiments
Myoglobin-CO Proximal Histidine Removed Vibrational Echo Experiments
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...
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
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
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
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
2016/5/23
Structural studies of carbonmonoxy myoglobin photolyzed at ultra-low temperatures have allowed the visualization of an otherwise elusive binding intermediate.
Spectroscopic Study of Ser92 Mutants of Human Myoglobin:Hydrogen Bonding Effect of Ser92 to Proximal His93 on Structure and Property of Myoglobin
Carbon Monoxide Cyanides Escherichia coli Ferric Compounds Ferrous Compounds Histidine Humans Hydrogen Bonding Magnetic Resonance Spectroscopy Mutagenesis Myoglobin Myoglobin Oxygen Polymerase Chain Reaction Recombinant Fusion Proteins Serine Serine Spectrophotometr Spectrum Analysis, Raman Structure-Activity Relationship
2016/5/23
Neutron diffraction studies have demonstrated that the hydroxyl group oxygen of Ser92(F7) is hydrogen bonded to the proximal His93(48) N epsilon H proton in myoglobin (Mb) [Cheng, X., & Shoenborn, B. ...
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.
Determination of the Carbon Monoxide Binding Constants of Myoglobin Mutants:Comparison of Kinetic and Equilibrium Methods
Binding Sites Carbon Monoxide Humans Kinetics Mutagenesis, Site-Directed Mutation Myoglobin Myoglobin Myoglobin Nitric Oxide Photolysis Protein Conformation Spectroscopy, Fourier Transform Infrared Structure-Activity Relationship
2016/5/23
The carbon monoxide (CO) binding constants of human myoglobin (Mb) and several single-site mutants have been determined using two different methods. In the kinetic method, which is commonly used for t...
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 ...
Ultrafast Measurements of Geminate Recombination of NO with Site-specific Mutants of Human Myoglobin
human myoglobin mutagenesis kinetics structure-function relationships picosecond timescale
2016/5/23
Flash photolysis studies of NO recombination to heme proteins offer a direct probe of protein structural changes on the tens of picoseconds timescale where they can be compared with molecular dynamics...