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. Author manuscript; available in PMC: 2014 Aug 1.
Published in final edited form as: Biochim Biophys Acta. 2013 Apr 2;1827(0):10.1016/j.bbabio.2013.03.010. doi: 10.1016/j.bbabio.2013.03.010

Fig. 1.

Fig. 1

A. The conformational switch found in the majority of known bCcP enzymes involves the reorganization of the distal face of the peroxidatic heme, as a function of the redox state of a high-potential heme, some 12 Å away. B. The mechanistic impact of reductive activation suggests that by “banking” an electron in the high potential center, the first kinetic intermediate need to involve the build-up of a radical species.