Abstract
Mössbauer, EPR, and biochemical techniques were used to characterize two dissimilatory sulfite reductases: desulforubidin fromDesulfovibrio baculatus strain DSM 1743 and desulfoviridin fromDesulfovibrio gigas. For each molecule of desulforubidin, there are two sirohemes and four [4Fe−4S] clusters. The [4Fe−4S] clusters are in the diamagnetic 2+ oxidation state. The sirohemes are high-spin ferric (S=5/2) and each siroheme is exchanged-coupled to a [4Fe−4S]2+ cluster. Such an exchange-coupled siroheme-[4Fe−4S] unit has also been found in the assimilatory sulfite reductase fromEscherichia coli/1/ and in a low-molecular weight sulfite reductase fromDesulfovibrio vulgaris/2/. For each molecule of defulfoviridin, there are two tetrahydroporphyrin groups and four [4Fe−4S]2+ clusters. To our surprise, we discovered that about 80% of the tetrahydroporphyrin groups, however, do not bind iron.
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Huynh, B.H., Moura, I., Lino, A.R. et al. Characterization of two dissimilatory sulfite reductases from sulfate-reducing bacteria. Hyperfine Interact 42, 905–908 (1988). https://doi.org/10.1007/BF02395536
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DOI: https://doi.org/10.1007/BF02395536