Department of Chemistry and Chemical Biology Cornell University, Baker Laboratory, 162 Sciences Drive, Ithaca, NY 14853, USA.
Department of Chemistry and Chemical Biology Cornell University, Baker Laboratory, 162 Sciences Drive, Ithaca, NY 14853, USA.
J Inorg Biochem. 2024 Nov;260:112682. doi: 10.1016/j.jinorgbio.2024.112682. Epub 2024 Jul 30.
The rate of photosynthesis and, thus, CO fixation, is limited by the rate of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Not only does Rubisco have a relatively low catalytic rate, but it also is promiscuous regarding the metal identity in the active site of the large subunit. In Nature, Rubisco binds either Mg(II) or Mn(II), depending on the chloroplastic ratio of these metal ions; most studies performed with Rubisco have focused on Mg-bound Rubisco. Herein, we report the first crystal structure of a Mn-bound Rubisco, and we compare its structural properties to those of its Mg-bound analogues.
光合作用的速率,进而 CO2 的固定速率,受到核酮糖-1,5-二磷酸羧化酶/加氧酶(Rubisco)的限速影响。Rubisco 的催化速率不仅相对较低,而且其大亚基活性部位的金属种类也很混杂。在自然界中,Rubisco 根据叶绿体中这些金属离子的比例,结合 Mg(II)或 Mn(II);Rubisco 的大多数研究都集中在结合 Mg 的 Rubisco 上。在此,我们报告了第一个结合 Mn 的 Rubisco 的晶体结构,并将其结构特性与结合 Mg 的类似物进行了比较。