PDF(Pubmed)
Abstract：
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO2) fixation in plants, which proceeds via the carboxylation of ribulose 1,5-biphosphate. Because of the enormous importance of this reaction in agriculture and the environment, there is considerable interest in the mechanism of fixation of CO2 by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 Å resolution. This structure is consistent with earlier single-crystal X-ray structures of this enzyme and the results are a good starting point for a further push towards time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.
摘要：
核酮糖-1,5-二磷酸羧化酶/加氧酶（RuBisCO）是负责植物中二氧化碳（CO2）固定的第一步的酶，通过1,5-二磷酸核酮糖的羧化进行。由于这种反应在农业和环境中的巨大重要性，对RuBisCO固定CO2的机制有相当大的兴趣。这里,据报道，菠菜RuBisCO的连续同步加速器晶体学结构为2.3µ分辨率。该结构与该酶的早期单晶X射线结构一致，该结果是进一步推动时间分辨连续同步加速器晶体学的良好起点，以便更好地了解反应机理。
