MAX IV Laboratory, Lund University, PO Box 118, 221 00 Lund, Sweden.
Department of Chemistry and Molecular Biology, University of Gothenburg, Medicinaregatan 9C, 413 90 Gothenburg, Sweden.
Acta Crystallogr F Struct Biol Commun. 2024 Jun 1;80(Pt 6):117-124. doi: 10.1107/S2053230X24004643. Epub 2024 May 29.
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO) 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 CO 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.
核酮糖-1,5-二磷酸羧化酶/加氧酶（RuBisCO）是植物中负责二氧化碳（CO）固定的第一步的酶，该过程通过核酮糖 1,5-二磷酸的羧化作用进行。由于该反应在农业和环境中的重要性，因此人们对 RuBisCO 固定 CO 的机制非常感兴趣。这里，报道了菠菜 RuBisCO 的一系列同步辐射晶体学结构，分辨率为 2.3 Å。该结构与该酶的早期单晶 X 射线结构一致，并且这些结果是进一步推动时间分辨同步辐射晶体学研究以更好地理解反应机制的良好起点。
