Structural highlights
Function
RBL_SPIOL RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
Publication Abstract from PubMed
The rate of photosynthesis and, thus, CO(2) 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.
The structure of Mn(II)-bound Rubisco from Spinacia oleracea.,Voland RW, Coleman RE, Lancaster KM J Inorg Biochem. 2024 Nov;260:112682. doi: 10.1016/j.jinorgbio.2024.112682. Epub , 2024 Jul 30. PMID:39094246[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Voland RW, Coleman RE, Lancaster KM. The structure of Mn(II)-bound Rubisco from Spinacia oleracea. J Inorg Biochem. 2024 Nov;260:112682. PMID:39094246 doi:10.1016/j.jinorgbio.2024.112682
