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  • Title: Dissimilatory sulfite reductase revisited. The desulfoviridin molecule does contain 20 iron ions, extensively demetallated sirohaem, and an S = 9/2 iron-sulfur cluster.
    Author: Marritt SJ, Hagen WF.
    Journal: Eur J Biochem; 1996 Jun 15; 238(3):724-7. PubMed ID: 8706673.
    Abstract:
    Assimilatory sulfite reductase contains a sirohaem that is very weakly coupled to a [4Fe-4S] cubane, i.e. five iron atoms in total. Dissimilatory sulfite reductase is a complex system with 20 Fe atoms/alpha 2 beta 2 gamma 2 hexamer. A recent revision of the purification procedure for the Desulfovibrio vulgaris dissimilatory enzyme has afforded a preparation of only 10 Fe atoms hexamer, this has led to the convulsion that the topology of prosthetic groups parallels that of the assimilatory system [Wolfe, B. M., Lui, S. M. & Cowan, J. A. (1994) Eur. J. Biochem. 223, 79-89]. The new purification procedure has been reproduced but the claimed molecular properties are not reproducible. The highly purified, active desulfoviridin contains 20, not 10, Fe atoms/molecule: the sirohaem is extensively dematallated, not metallated; and the S = 9/2 iron-sulfur cluster is present, not absent.
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