CHALCOGEN AMINO ACID ANALOGS IN PHASE DETER IN XRAY PROTEIN CRYSTALLOGRAPHY

X 射线蛋白质晶体学中的相位延迟中的硫属氨基酸类似物

• 批准号: 6120832
• 负责人: THIERRY FISCHMANN
• 金额: $ 1.54万
• 依托单位: UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-01-15 至 2000-01-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6120832
• 关键词: biological products; biomedical resource; enzymes; human tissue; plants

The SIR provided D,L- [Ring- "N2]Histidine; Ig Difference infrared spectroscopy can be used to identify structural changes that occur in electron transfer proteins upon charge separation. In photosystern II, the photosynthetic oxygen evolving complex, a redox active tyrosine residue, Z, plays an important role in the electron transfer events that precede oxygen evolution. A stable tyrosine radical is also present in the enzyme; this second redox active tyrosine, D, has no known function. We are using vibrational spectroscopy to investigate the structural differences between D and Z. We have obtained the vibrational difference spectrum associated with the oxidation of each tyrosine. This can be done because the decay kinetics of the two radicals differ by many orders of magnitude. The spectra associated with the oxidation of D and Z are different, and the observed spectral differences are consistent with the conclusion that there is a difference in hydrogen bonding to the phenol oxygens of the two tyrosines. Such a difference in hydrogen bonding could help to explain the observed functional differences between D and Z. Use of 180 tyrosine is an important component of our studies, since it will allow us to label the tyrosine residues in vivo. In turn, this labeling will allow us to definitively assign lines in the vibrational spectrum to the C-0 stretch of the radical and to the C-OH stretch of the neutral residue. These studies are in progress.

SIR提供D，L- [环-N2]组氨酸; IG差异红外 光谱学可用于识别发生在细胞中的结构变化， 电子转移蛋白质的电荷分离。 在摄影系统中 II，光合放氧复合物，氧化还原活性 酪氨酸残基Z在电子转移中起重要作用 在氧气释放之前的事件。 稳定的酪氨酸自由基是 也存在于酶中;这种第二氧化还原活性酪氨酸D具有 没有已知的功能。 我们用振动光谱学 研究D和Z之间的结构差异。我们有 获得了与振动相关的振动差谱。 每种酪氨酸的氧化。 这是可以做到的，因为腐烂 两种自由基的动力学相差许多数量级。 的 与D和Z的氧化相关的光谱是不同的，并且 观察到的光谱差异与结论一致 与酚氧的氢键有所不同 两种酪氨酸的区别 氢键的这种差异 有助于解释D和Z之间观察到的功能差异。 使用180酪氨酸是我们研究的重要组成部分，因为它 将使我们能够在体内标记酪氨酸残基。 这又 标记将使我们能够明确地分配振动中的线， 光谱到自由基的C-O伸缩和自由基的C-OH伸缩 中性残留物。 这些研究正在进行中。