Max Planck Institute for Terrestrial Microbiology, Department of Biochemistry and Synthetic Metabolism, Karl-von-Frisch-Str. 10, 35043 Marburg, Germany.
Max Planck Institute for Terrestrial Microbiology, Department of Biochemistry and Synthetic Metabolism, Karl-von-Frisch-Str. 10, 35043 Marburg, Germany.
Curr Opin Biotechnol. 2018 Feb;49:100-107. doi: 10.1016/j.copbio.2017.07.017. Epub 2017 Aug 29.
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) is arguably one of the most abundant proteins in the biosphere and a key enzyme in the global carbon cycle. Although RubisCO has been intensively studied, its evolutionary origins and rise as Nature's most dominant carbon dioxide (CO)-fixing enzyme still remain in the dark. In this review we will bring together biochemical, structural, physiological, microbiological, as well as phylogenetic data to speculate on the evolutionary roots of the CO-fixation reaction of RubisCO, the emergence of RubisCO-based autotrophic CO-fixation in the context of the Calvin-Benson-Bassham cycle, and the further evolution of RubisCO into the 'RubisCOsome', a complex of various proteins assembling and interacting with the enzyme to improve its operational capacity (functionality) under different biological and environmental conditions.
核酮糖-1,5-二磷酸羧化酶/加氧酶(RubisCO)可以说是生物圈中最丰富的蛋白质之一,也是全球碳循环中的关键酶。尽管 RubisCO 已经被深入研究,但它的进化起源和作为自然界中最占主导地位的二氧化碳(CO)固定酶的出现仍然不清楚。在这篇综述中,我们将结合生化、结构、生理、微生物学以及系统发育数据,推测 RubisCO 的 CO 固定反应的进化根源、RubisCO 为基础的 Calvin-Benson-Bassham 循环中的自主 CO 固定的出现,以及 RubisCO 进一步进化为“RubisCO 体”,即各种蛋白质组装并与酶相互作用的复合物,以在不同的生物和环境条件下提高其操作能力(功能性)。