Structure of fluoride methemoglobin

Spectral, Conformational and Chemical Properties of Opossum Methemoglobin

“…5 F). These observations further confirm the idea that a number of different tertiary conformations are possible in a given quaternary state [16,24].…”

“…Ascorbic acid produces absorbance changes corresponding to about 50 reduction in methemoglobin A (dA = 0.12) and 100% reduction in methemoglobin opossum ( A A = 0. 24) proceeds in a linear fashion while in its presence the reaction is biphasic. On the other hand opossum methemoglobin reduction is biphasic in the absence of P6-inositol and monophasic in its presence (Fig.7).…”

Electron Spin–Lattice Relaxation Rates for High-Spin Fe(III) Complexes in Glassy Solvents at Temperatures between 6 and 298 K

“…Modulation of the zero-field splitting by motion of the axial ligands is likely to be a significant contribution to the relaxation. In the heme proteins, the axial ligands are hydrogen bonded (51,52) to water molecules or protein side chains, which substantially restricts the motional freedom of the ligands compared with that in the small molecules, which may account for the smaller coefficients, A Orb and A Orb2 . Similarly, in studies of S ϭ 1 2 complexes it was observed that the coefficients of the Raman process were larger for more flexible molecules than for rigid molecules (27,53).…”

Iron Coordination Structures of Oxygen Sensor FixL Characterized by Fe K-edge Extended X-ray Absorption Fine Structure and Resonance Raman Spectroscopy

“…In addition, it is also puzzling that the iron in the metF Ϫ complex of Aplysia Mb has been reported to be located in the heme plane (in-plane configuration), despite the high spin heme iron. On the other hand, Deatherage et al (45) reported the structural change of metHb induced by the F Ϫ binding based on x-ray difference Fourier technique, which showed that the F Ϫ binding to the met iron as a sixth ligand causes a small movement of the iron toward the porphyrin plane.…”