Abstract
In order to more fully understand the redox chemistry of ironsulfur proteins and to test specifically the three-state hypothesis for the super-reduction of the Fe 4 S 4 * cluster, the electrochemistry for both Chromatium vinosum and Rhodopseudomonas gelatinosa high potential iron-sulfur proteins (HiPIP) was studied. Cyclic voltammetry and related experiments demonstrated the involvement of an adsorption process and an adsorption mechanism was proposed for the observed electrochemistry. The electrochemistry of apo -HiPIP (HiPIP without the cluster) was examined and compared to native HiPIP. A new catalytic Brdička current was found for HiPIP in which there are no free sulfhydryl or disulfide bonds but only Fe−S (S from cysteine) and Fe−S * (S * =inorganic sulfide) bonds.
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