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. Author manuscript; available in PMC: 2010 Feb 1.
Published in final edited form as: J Biol Inorg Chem. 2008 Oct 16;14(2):179–191. doi: 10.1007/s00775-008-0436-x

Figure 7.

Figure 7

Correlation of Fe-CO and C-O stretching frequencies for different heme proteins and porphyrin derivatives. Lines (1) and (2) are for complexes in which the proximal ligand is thiolate and histidine, respectively. Line (3) is for five-coordinate CO adducts. The open circles, open squares and open triangles correspond to data obtained for mutant and pH-variant forms of horse radish peroxidase, cytochrome c peroxidase and myoglobin, respectively. The corresponding filled symbols represent data obtained from the wild-type proteins. The filled and open diamonds correspond to wild-type NP1 and the mutant H59C_NP1 data, respectively, measured in this work. Figure adapted from refs. (63,65,66).