Effect of pH on the thermostability and redox properties of cytochrome c552 from Wolinella succinogenes
Mordido, V. H.; Carepo, M. S. P.; Cordas, C. M.; Paul, N.; Simon, J.; Moura, I.; Pauleta, S. R.
Show abstract
Cytochrome c552 from Wolinella succinogenes is one of the few examples of a low reduction potential class I c-type cytochrome with a mixture of high/low spin state populations observed in its visible spectrum. Analysis of its structural model suggests that the heme is Met/His coordinated and highly solvent-exposed. This supports the hypothesis that it is the solvent accessibility of the propionate groups that controls the reduction potential of small c-type cytochromes. The visible spectra obtained at different pH values reveal the presence of a protonable group with a pKa of 7.3, which also influences the reduction potential of this small cytochrome c552 (Em0 of 97 {+/-} 5 mV, pH 7.0) and can be either an H2O/OH- group distantly coordinating the heme iron, or one of the propionate groups. The thermostability of cytochrome c552 has been studied by circular dichroism and differential scanning calorimetry, indicating a highly stable protein at pH 5-7 (90 {degrees}C to 77 {degrees}C).
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