References

1. K. Sugiyama, R. Highet, A. Woods, R. Cotter, Osawa Y, (1997). Hydrogen peroxide-meditated alteration of the heme prosthetic group ofmetmyoglobin to an iron chlorine product: Evidence for a novel oxidativepathways: Biochemistry v.94:796-801

2.Sugawara Y, Matsuoka A,Kaino A, Shikama K (1995). Role of Globin Moiety in theAutoxidation Reaction of Oxymyoglobin: Effect of 8 M Urea. Biophysical Journal v.69:583-592

3. D. Livingston, S. McLachlan, G. La Marl, W. Brown (1985). Myoglobin: Cytochromeb5 interactions and the Kinetic Mechanism of Metmyoglobin Reductase: Journal of Biological Chemistry v.260: 15699-15707

4. Hubbard S,Hendrickson W, David G (1990). X-ray crystalstructure of a recombinant human myoglobin mutant at 2.8 A resolution. J.Mol.Biol. 213,215-218

5. Adachi S, Nagano S, Ishimori K, Watanabe Y, Morishima I, Egawa T,Kitagawa T, Makino R (1993). Rolesof proximal ligand in heme proteins: replacement of proximal histidine of humanmyoglobin with cysteine and tyrosine by site-directed mutagenesis as models forP-450, chloroperoxidase, and catalase. Biochemistryv.32:241-252

6. Rovira C (2003). The structure and dynamics of theFe-CO bond in myoglobin. Journal of Physics: Condensed matter.S1809-S1822

7. Dou Y, AdmiraalS, Ikeda-Saito M, Krzywda S, Wilkinson A, Li T, Olson J, Prince R, Pickering I,George G (1995). Alteration of axial coordination by proteinengineering in myoglobin. Bisimidazole ligation inthe His64-->Val/Val68-->His double mutant. J Biol Chem.270: 15993-6001

8. Anderton C,Hester R, Moore J (1995). Resonance Ramanspectroscopy reveals novel ligation properties of the porcine myoglobin doublemutant H64V/V68H. Biochem Biophysics Acta 1253(1):1-4.