Yamamoto T, Palmer G, Crespi H
Biochim Biophys Acta. 1976 Jul 19;439(1):232-9. doi: 10.1016/0005-2795(76)90178-1.
A c type cytochrome isolated from Synechococcus lividus grown on water and 2H2O media, has been studied by resonance Raman spectroscopy. The spectra were taken on the oxidized and reduced protein with excitation within the Soret band at 441.6 nm to determine whether individual resonance Raman bands of the heme shift upon deuterium substitution and also to provide a comparison with the spectra of horse heart cytochrome c. Some of the shifts observed with the deuterated heme c are larger than the corresponding shifts in meso-deuterated metalloporphyrins suggesting mixing of peripheral substituent vibrations with the skeletal modes of the porphyrin macrocycle. The algal cytochrome exhibits resonance Raman spectra roughly similar to those of horse heart cytochrome c, consistent with its optical absorption spectra which is typical of c type cytochromes, although a detailed comparison reveals note-worthy differences between the spectra of the two proteins; this may be a reflection of the effect of non-methionine ligands and protein environment on the vibrations of the c type heme in the algal cytochrome.
从生长在水和2H₂O培养基上的蓝藻中分离出的一种c型细胞色素，已通过共振拉曼光谱进行了研究。在441.6 nm的Soret带内激发下，对氧化态和还原态蛋白质进行了光谱测定，以确定血红素的各个共振拉曼带在氘取代后是否发生位移，并与马心血红素c的光谱进行比较。氘代血红素c观察到的一些位移大于中-氘代金属卟啉中的相应位移，这表明外围取代基振动与卟啉大环的骨架模式发生了混合。藻类细胞色素的共振拉曼光谱与马心血红素c的光谱大致相似，这与其典型的c型细胞色素的光吸收光谱一致，尽管详细比较发现这两种蛋白质的光谱之间存在显著差异；这可能反映了非甲硫氨酸配体和蛋白质环境对藻类细胞色素中c型血红素振动的影响。
