The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate.

@article{Duff2000TheTB,
  title={The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate.},
  author={Anthony P. Duff and Timothy J. Andrews and Paul M. G. Curmi},
  journal={Journal of molecular biology},
  year={2000},
  volume={298 5},
  pages={903-16}
}
d-Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyses the central CO(2)-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… CONTINUE READING
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