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High Yield of M-Side Electron Transfer in Mutants of Rhodobacter Capsulatus Reaction Centers Lacking the L-Side Bacteriopheophytin
Rhodobacter capsulatus Pheophytins Detergents Spectrum Analysis Oxidation-Reduction Mutation Plasmids Amino Acid Sequence Molecular Sequence Data Histidine
2016/5/24
We present studies on a series of photosynthetic reaction center (RC) mutants created in the background of the Rhodobacter capsulatus D(LL) mutant, in which the D helix of the M subunit has been subst...
Energetics of Primary Charge Separation in Bacterial Photosynthetic Reaction Center Mutants:Triplet Decay in Large Magnetic Fields
horseradish peroxidase lignin peroxidase enzymatic oxidations N-demethylation methylene blue azure B azure C
2016/5/24
The triplet state of aromatic molecules forms and decays by intersystem crossing, as originally demonstrated by Kasha and Lewis. By contrast, the triplet state of the primary electron donor, 3 P, in p...
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...
Excited State Electronic Asymmetry of the Special Pair in Photosynthetic Reaction Center Mutants:Absorption and Stark Spectroscopy
Dimerization Electron Transport Electrons Hydrogen Bonding Models, Chemical Mutagenesis, Site-Directed Oxidation-Reduction Photosynthetic Reaction Center Complex Proteins Rhodobacter sphaeroides Spectrophotometry Static Electricity
2016/5/23
The electronic absorption line shape and Stark spectrum of the lowest energy Q(y)() transition of the special pair in bacterial reaction centers contain a wealth of information on mixing with charge t...
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...
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. ...
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...
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...
Dynamics of Protein Relaxation in Site-Specific Mutants of Human Myoglobin
Humans Cysteine Heme Alanine Myoglobin Recombinant Proteins Spectrophotometry Mutagenesis,Site-Directed Amino Acid Sequence Protein Conformation
2016/5/23
We have recently reported spectroscopic evidence for structural relaxation of myoglobin (Mb) following photodissociation of MbCO [Lambright, D. G., Balasubramanian, S., & Boxer, S. G. (1991) Chem. Phy...
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...
CO Recombination to Human Myoglobin Mutants in Glycerol-Water Solutions
CO Recombination Human Myoglobin Mutants Glycerol-Water Solutions
2016/5/23
The kinetics of CO recombination to site-specific mutants of human myoglobin have been studied by flash photolysis in the temperature range 250-320 K on the nanosecond to second time scale in 75% glyc...
Spectroscopic and Redox Properties of Sym1 and (M)F195H Rhodobacter capsulatus Reaction Center Symmetry Mutants Which Affect the Initial Electron Donor
Circular Dichroism Electron Spin Resonance Spectroscopy Electron Transport Genes, Bacterial Kinetics Light-Harvesting Protein Complexes Mutation Oxidation-Reduction Photosynthetic Reaction Center Complex Proteins Plasmids Protein Conformation Rhodobacter capsulatus Spectrophotometry
2016/5/23
The redox properties, absorption, electroabsorption, CD, EPR, and P+QA- recombination kinetics have been measured for the special pairs of two mutants of Rhodobacter capsulatus reaction centers involv...
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 ...