REVISION OF THE HEME-CORE ARCHITECTURE IN THE TETRAHEAM CYTOCHROME C3 FROM DESULFOVIBRIO-BACULATUS BY 2-DIMENSIONAL H-1-NMR

The haem-core architecture in cytochrome C3 isolated from Desulfovibrio baculatus (Norway 4) was probed using two-dimensional H-1 NMR. Interhaem connectivities detected in NOE spectroscopy experiments performed at short mixing times are incompatible with the structure of the protein determined by X-ray crystallography, but agree instead with the haem arrangement found in cytochrome C3 from Desulfovibrio vulgaris (Miyazaki). These experiments show unequivocally that the relative orientation of the four haems in the two proteins is the same and does not involve the 180-degrees rotation of haems I and IV indicated in the X-ray structure determined for the cytochrome c3 from D. baculatus (Norway 4).