The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
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Duff, Anthony; Andrews, Thomas; Curmi, Paul
Description
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]
Collections | ANU Research Publications |
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Date published: | 2000 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/90228 |
Source: | Journal of Molecular Biology |
DOI: | 10.1006/jmbi.2000.3724 |
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