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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 ...
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 ...
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...
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...
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...
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...
Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by ...
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...
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...
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...
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...
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...
Structural studies of carbonmonoxy myoglobin photolyzed at ultra-low temperatures have allowed the visualization of an otherwise elusive binding intermediate.

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