EPR spectroscopy of the iron-sulphur cluster and sirohaem in the dissimilatory sulphite reductase (desulphoviridin) from Desulphovibrio gigas.
Desulphoviridin in the oxidized state showed EPR signals around g = 6, consistent with the sirohaem being in the high-spin ferric state. This was unreactive with sulphite, sulphide or cyanide; but readily reduced by methyl viologen. When the enzyme was treated with Na2S2O4 the sirohaem was slowly reduced and a spectrum of a reduced iron-sulphur cluster at g = 2.07, 1.93, 1.91 appeared over the course of an hour. An intermediate in this reaction was indicated by a free radical signal which appeared within seconds and then gradually disappeared. On treatment with nitrite and reduced methyl viologen, the enzyme gave a spectrum of a nitroxide derivative similar to that seen with plant nitrite reductase. The midpoint reduction potential of the haem was estimated to be -310 mV or less. The iron-sulphur cluster has a very low potential, being only reduced in the presence of free Na2S2O4 around -560 mV. Desulphoviridin can be classed with sirohaem-containing iron-sulphur proteins.
D001665:Binding Sites; D003901:Desulfovibrio / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D011485:Protein Binding; D011487:Protein Conformation
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors