MacDonald G M, Bixby K A, Barry B A
Department of Biochemistry, University of Minnesota, St. Paul 55108.
Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11024-8. doi: 10.1073/pnas.90.23.11024.
Photosystem II, the photosynthetic water-oxidizing complex, contains two redox-active tyrosine residues. Although current models suggest that these tyrosines are located in symmetric positions in the reaction center, there are functional differences between them. To elucidate those structural factors that give rise to this functional asymmetry, we have used difference Fourier-transform infrared spectroscopy to obtain the vibrational difference spectrum associated with the oxidation of each of these redox-active residues. Isotopic labeling was employed to definitively assign vibrational lines to the redox-active tyrosines. This work has shown that the vibrational spectra of the two redox-active species are significantly different from each other. This result suggests that the structure of the redox-active residue helps to determine its role in electron transfer in the reaction center.
光系统II,即光合水氧化复合体,包含两个具有氧化还原活性的酪氨酸残基。尽管目前的模型表明这些酪氨酸在反应中心处于对称位置,但它们之间存在功能差异。为了阐明导致这种功能不对称的结构因素,我们使用了差分傅里叶变换红外光谱来获得与这些氧化还原活性残基各自氧化相关的振动差谱。采用同位素标记来明确将振动谱线归属于氧化还原活性酪氨酸。这项工作表明,这两种氧化还原活性物质的振动光谱彼此显著不同。这一结果表明,氧化还原活性残基的结构有助于确定其在反应中心电子转移中的作用。