@article {2592,
	title = {Characterization of two dissimilatory sulfite reductases from sulfate-reducing bacteria},
	journal = {Hyperfine Interactions},
	volume = {42},
	number = {1},
	year = {1988},
	note = {n/a},
	pages = {905-908},
	publisher = {Springer Netherlands},
	abstract = {<p>M{\"o}ssbauer, EPR, and biochemical techniques were used to characterize two dissimilatory sulfite reductases: desulforubidin from Desulfovibrio baculatus strain DSM 1743 and desulfoviridin from Desulfovibrio 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 from Escherichia coli /1/ and in a low-molecular weight sulfite reductase from Desulfovibrio 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.</p>
},
	keywords = {Physics and Astronomy},
	isbn = {0304-3843},
	url = {http://dx.doi.org/10.1007/BF02395536},
	author = {Huynh, B. and Moura, I. and Lino, A. and Moura, J. and Legall, J.}
}
