Fe-heme structure and dynamics in Thr72 → Ile mutant Scapharca inaequivalvis hemoglobin by X-ray absorption spectroscopy

Polarized X-ray absorption spectroscopy of the low-temperature photoproduct of carbonmonoxy-myoglobin

Polarized X-ray absorption spectra of single crystals (0.2 × 0.2 × 0.2 mm) of carbonmonoxy myoglobin and its cryogenic photoproduct at T = 20 K have been collected in fluorescence mode. The data can be interpreted to provide insight into both the structural and electronic changes at the Fe-heme site level