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. Author manuscript; available in PMC: 2009 Oct 31.
Published in final edited form as: J Inorg Biochem. 2007 Aug 25;102(2):216–233. doi: 10.1016/j.jinorgbio.2007.08.002

Fig. 4.

Fig. 4

A superposition of the heme environments in the crystal structures of hh MnIIIMb(H2O) (this work, shown in light grey) and hh MnIIMb (this work, shown in dark grey) using a global Cα structural alignment, and shown from two different views. The Nε atoms of the His64 and His93 residues of MnIIMb are shifted from their major/minor positions in MnIIIMb(H2O) by 0.95/0.21 and 0.37 Å, respectively. Also, the MnII center is shifted 0.25 Å from its MnIII position. A meso carbon and its connecting pyrrole ring A are shifted towards the proximal side in MnIIMb relative to those in MnIIIMb(H2O).