Ring-fluorinated haem

NMR Studies of A-Type Haemoproteins Reconstituted with a Ring-Fluorinated Haem... 

The volume begins with an account of Applications of Si NMR Parameters by B. Wrackmeyer Y. Yamamoto reports on NMR Studies of 6-Type Haemoproteins Reconstituted with a Ring-Fluorinated Haem Site Directed Sohd State NMR on Membrane Proteins is covered by H. Saito W. Kremer reports on High Pressure NMR Studies in Proteins and the volume is completed with an account of Xenon NMR Spectroscopy by D. Raftery. 

The electronic structures of the porphyrins were compared through the analysis of the H NMR spectra of their dimethyl ester derivatives (Fig. 4). The fluorinated porphyrins exhibited typical spectral patterns similar to those of protoporphyrin and mesoporphyrin. In general, the shifts of the signals are affected by the ring current of the porphyrin macrocycle and the electronic inductive effect of nearby substituents and the ring-current shift is also modulated by the electronic contribution of the substituents. Since four meso protons, namely, protons bound to carbons at the 5, 10, 15, and 20 positions occupy the same orientation relative to the porphyrin macrocycle, in-plane asymmetry of the haem electronic structure is reflected directly... 

S — 5/2) reconstituted with 3,7-DF was characterized in order to evaluate relaxation mechanism in the protein with a variety of magnetic properties (Fig. 40). Since the fluorine atoms introduced to 3,7-DF are dynamically fixed to the porphyrin ring, analysis of the field strength dependence of the line width of the F signals provides the correlation time (tr) of the haem accommodated in the active site of Mb. 

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