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Title: Characterization of a sulfite reductase from Desulfovibrio vulgaris

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:5332045

A low-molecular-weight (M/sub r/ = 27,200) sulfite reductase from Desulfovibrio vulgaris was studied with Moessbauer, EPR, and chemical techniques. This sulfite reductase was found to contain one siroheme and one (4Fe-4S) cluster. As purified, the siroheme is low-spin ferric (S = 1/2) which exhibits characteristic EPR resonances at g = 2.44, 2.36, and 1.77. At 150 K, the observed Moessbauer parameters, ..delta..E/sub Q/ = 2.49 +/- 0.02 mm/s and delta = 0.31 +/- 0.02 mm/s, for the siroheme are typical for low-spin ferric complexes. The (4Fe-4S) cluster is in the 2+ state. The Moessbauer parameters, ..delta..E/sub Q/ = 0.95 +/- 0.02 mm/s and delta = 0.38 +/- 0.02 mm/s, for the cluster are almost identical to those observed for the (4Fe-4S)/sup 2 +/ cluster in the hemoprotein subunit of the sulfite reductase from Escherichia coli. Similar to the hemoprotein subunit of E. coli sulfite reductase, low-temperature Moessbauer spectra of D. vulgaris sulfite reductase recorded with weak and strong applied fields also show evidence for an exchange-coupled siroheme-(4Fe-4S) unit. 31 references, 4 figures, 1 table.

Research Organization:
Emory Univ., Atlanta, GA
DOE Contract Number:
AS09-79ER10499
OSTI ID:
5332045
Journal Information:
J. Biol. Chem.; (United States), Vol. 259:24
Country of Publication:
United States
Language:
English