Elucidation of mechanisms of bilin synthesizing enzyme and photo-adaptation regulating protein

我们试图通过晶体结构来阐明合成胆磷脂色素的酶PcyA的分子机制。这些研究包括PcyA突变体的分析、中子晶体学和x射线晶体学。PcyA的特点在于它依次还原胆绿素的两个位点。当第一步完成后，PcyA切换到第二步。我们确定了Asp105和其他残基参与了该反应。测定了Asp105和胆绿素的质子化状态，并阐明了还原的分子机制。我们成功地结晶了全长蓝藻色素。

We tried to elucidate the molecular mechanism of PcyA, an enzyme that synthesize bilin pigment, through crystal structures. These studies include analysis of PcyA mutants and neutron crystallography as well as X-ray crystallography. PcyA is characteristic in that it reduces two sites of biliverdin sequentially. When the first step is completed, PcyA switches to the second step. We defined Asp105 and other residues are involved in this reaction. We also determined the protonation state Asp105 and biliverdin, and clarified the molecular mechanisms of the reduction.We succeeded in crystallization of the full-length cyanobacteriochrome.