Electron paramagnetic resonance and magnetic circular dichroism studies of a hexa-heme nitrite reductase from Wolinella succinogenes.
The nature of the heme centers in the hexa-heme dissimilatory nitrite reductase from the bacterium Wolinella succinogenes has been investigated with EPR and magnetic circular dichroism spectroscopy. The EPR spectrum of the ferric enzyme is complex showing, in addition to magnetically isolated low-spin ferric hemes with g values of 2.93, 2.3 and 1.48, two sets of signals at g = 10.3, 3.7 and 4.8, 3.21, which we assign to two pairs of exchange coupled hemes. The MCD spectra show that the isolated hemes are bis-histidine coordinated and that there is one high-spin ferric heme. The exchange coupling is lost on treatment with SDS.
D001421:Bacteria, Anaerobic / Q000201:enzymology*; D002942:Circular Dichroism / Q000379:methods; D004578:Electron Spin Resonance Spectroscopy; D005290:Ferric Compounds / Q000032:analysis; D006418:Heme / Q000032:analysis; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis*; D009572:Nitrite Reductases / Q000032:analysis*; D011485:Protein Binding
D005290:Ferric Compounds; D006418:Heme; D009247:NADH, NADPH Oxidoreductases; D009572:Nitrite Reductases