Mössbauer study of cytochrome c2 from Rhodospirillum rubrum. Sign of the product gxgygz of some low spin ferric heme proteins.
We have studied cytochrome c2 from Rhodospirllum rubrum with Mössbauer spectroscopy and electron paramagnetic resonance. The Mössbauer data on the ferric protein, taken in external magnetic fields up to 50 kG, were analyzed within the framework of the ligand field model commonly used to evaluate low-spin ferric heme compounds. The data analysis shows that the determinant of the electronic g-tensor, i.e. the product gxgygz, is positive for cytochrome c2. We have reanalyzed published Mössbauer data of some low-spin ferric heme proteins with respect to the sign of the g-tensor determinant. We find that gxgygz is also positive for the cytochromes c, bs, and P-450, and for chloroperoxidase.
D003574:Cytochrome c Group; D004578:Electron Spin Resonance Spectroscopy; D006420:Hemeproteins; D007501:Iron; D008433:Mathematics; D011487:Protein Conformation; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D013057:Spectrum Analysis
D003574:Cytochrome c Group; D006420:Hemeproteins; D007501:Iron