The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
D-Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyses the central CO2-fixing reaction of photosynthesis in a complex, multiple-step process. Several structures of rubisco complexed with substrate analogues, inhibitors and products have been determined by X-ray crystallography. The structures fall into two well-defined and distinct states. The active site is either 'open' or 'closed'. The timing and mechanism of the transition between these two states have been uncertain. We...[Show more]
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|Source:||Journal of Molecular Biology|
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