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Symbiotic relationships between legumes and the bacteria that grow in their roots are critical for plant survival. Without those bacteria, the plants would have no source of nitrogen, an element that ...
Heme,a Poisonous Nutrient,Tracked by‘Green Lantern’Sensor
Heme Poisonous Nutrient Tracked Green Lantern Sensor
2016/6/12
In minuscule amounts, it works in cells as an essential catalyst called a cofactor and as a signaling molecule to trigger other processes. Now, for the first known time, researchers have tracked those...
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...
Vibrational Stark Spectroscopy of NO Bound to Heme:Effects of Protein Electrostatic Fields on the NO Stretch Frequency
rare earth alloys X-ray diffraction crystal structure phase diagram
2016/5/23
The vibrational Stark effect measures the effect of an external electric field on the vibrational (IR) spectrum of a molecule. This technique gives quantitative information on the sensitivity of a vib...
Resonance Raman Studies of Heme Axial Ligation in H93G Myoglobin
chemical vapor deposition diamond electron microscopy epitaxy iridium surface structure,morphology,roughness,and topography
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
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 ...
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...
Stark Effect Spectroscopy of the Heme Charge Transfer Bands of Deoxymyoglobin
materials science electronic structure oxygen compounds myoglobin charge transport stark effect absorption spectra spectroscopy heme protoporphyrins
2016/5/23
We report the Stark spectra of the Soret, Q, and charge-transfer bands of deoxymyoglobin. The data show that band III has charge-transfer character but that the magnitude of the charge displacement is...
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
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...
Vibrational Dynamics of Carbon Monoxide at the Active Sites of Mutant Heme Proteins
Vibrational Dynamics Carbon Monoxide Active Sites Mutant Heme Proteins
2016/5/23
Picosecond mid-IR pump−probe measurements of vibrational relaxation (VR) of CO bound to the active sites of wild-type and mutant myoglobins (Mb) reveal that an approximately linear relationship ...
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...
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...
Effect of Heme Oxygenase-1 on the smooth muscle cells growth
Heme Oxygenase-1 muscle cells
2014/3/31
Infection of SMCs with AdHO-1 inhibit the proliferative response to serum in a concentration-dependent manner,the effect of HO-1 on the smooth muscle cells growth.