Myoglobin reconstituted

Hayashi T, Dejima H, Matsuo T et al (2002) Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. J Am Chem Soc 124 11226-11227... 

Hayashi T, Murata D, Makino M (2006) Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene. Inorg Chem 45 10530-10536... 

Monzani E, Alzuet G, Casella L et al (2000) Properties and reactivity of myoglobin reconstituted with chemically modified protohemin complexes. Biochemistry 39 9571-9582... 

Trematode species from paramphistomum epiclitum. At 25 °C, pH 7.0. Sperm whale. Horse heart. Myoglobin reconstituted with an ironporphycene. At 25 °C, pH 7.0. 

Matsuo T, Hayashi T, Hisaeda Y. Reductive Activation of dioxygen by a myoglobin reconstituted with a flavohemin. J. Am. Chem. Soc. 2002 124 11234-11235. 

Figure 43. (A) Electron-transfer pathway for the cyclic photoinduced hydrogenation of acetylene by lactate using eosin-modified myoglobin reconstituted with Co(II)-protoporphyrin IX working in cooperation with LDH. (B) Rates of formation of products upon illumination of a photosystem composed of myoglobin reconstituted with Co(II)-protoporphyrin IX and modified with eosin (0.11 mg mL ), LDH (0.6 units mL ), 5 (8 x 10 M) and lactic acid (1 x 10 M) under an atmospheric pressure of acetylene (a) rate of ethylene formation and (b) rate of pyruvic acid formation. (C) Hypothetical improved system for the same photobiocatalytic system, where the two enzymes and electron mediator are covalently linked.

Figure 46. Interprotein photo-induced electron transfer in a system composed of positively charged cytochrome c and myoglobin reconstituted with Zn-protoporphyrin IX covalently bound to a negatively charged comb providing association of the proteins in the assembly.

Figure 8. Infrared difference spectra of carbonyl sperm whale myoglobins reconstituted from different hemes vs. metmyoglobin in phosphate buffer, pH 6 4, Top protoheme. Middle deu-teroheme. Bottom mesoheme.

Properties of Myoglobins Reconstituted with Fluorinated Haems... 

NMR SPECTRAL PROPERTIES OF MYOGLOBINS RECONSTITUTED WITH FLUORINATED HAEMS... 

D. A. Simmons and L. Konermann, Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-hne isotope-pulse labeling. Biochemistry 42, 1906-1914 (2002). 

Simmons, D.A., Konermann, L. (2002) Characterization of Transient Protein Folding Intermediates during Myoglobin Reconstitution by Time-resolved Electrospray Mass Spectrometry with On-hne Isotopic Pulse Labeling. Biochemistry 41 1906-1914. 

Fig. 11 Schematic cartoons of myoglobin reconstituted with two photosensitisers. A Apomyoglobin-hypericin complex. B Zn(ii)-protoporphyrin IX-substituted myoglobin. ...

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