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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...
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 ...
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...
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...
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...

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