Efficient ion-photon qubit SWAP gate in realistic ion cavity-QED systems without strong coupling

We present a scheme for deterministic ion-photon qubit exchange, namely a SWAP gate, based on realistic cavity-QED systems with 171Yb+, 40Ca+ and 138Ba+ ions. The gate can also serve as a single-photon quantum memory, in which an outgoing photon heralds the successful arrival of the incoming photonic qubit. Although strong coupling, namely having the single-photon Rabi frequency be the fastest rate in the system, is often assumed essential, this gate (similarly to the Duan-Kimble C-phase gate) requires only Purcell enhancement, i.e. high single-atom cooperativity. Accordingly, it does not require small mode volume cavities, which are challenging to incorporate with ions due to the difficulty of trapping them close to dielectric surfaces. Instead, larger cavities, potentially more compatible with the trap apparatus, are sufficient, as long as their numerical aperture is high enough to maintain small mode area at the ion's position. We define the optimal parameters for the gate's operation and simulate the expected fidelities and efficiencies, demonstrating that efficient photon-ion qubit exchange, a valuable building block for scalable quantum computation, is practically attainable with current experimental capabilities.Comment: 18 pages, 9 figure

The role of BST4 in the pyrenoid of Chlamydomonas reinhardtii

ABSTRACT In many eukaryotic algae, CO2 fixation by Rubisco is enhanced by a CO2- concentrating mechanism, which utilizes a Rubisco-rich organelle called the pyrenoid. The pyrenoid is traversed by a network of thylakoid-membranes called pyrenoid tubules, proposed to deliver CO2. In the model alga Chlamydomonas reinhardtii ( Chlamydomonas ), the pyrenoid tubules have been proposed to be tethered to the Rubisco matrix by a bestrophin-like transmembrane protein, BST4. Here, we show that BST4 forms a complex that localizes to the pyrenoid tubules. A Chlamydomonas mutant impaired in the accumulation of BST4 ( bst4 ) formed normal pyrenoid tubules and heterologous expression of BST4 in Arabidopsis thaliana did not lead to the incorporation of thylakoids into a reconstituted Rubisco condensate. Chlamydomonas bst4 mutant did not show impaired growth at air level CO2. By quantifying the non-photochemical quenching ( NPQ ) of chlorophyll fluorescence, we show that bst4 displays a transiently lower thylakoid lumenal pH during dark to light transition compared to control strains. When acclimated to high light, bst4 had sustained higher NPQ and elevated levels of light-induced H2O2 production. We conclude that BST4 is not a tethering protein, but rather is an ion channel involved in lumenal pH regulation possibly by mediating bicarbonate transport across the pyrenoid tubules. One-sentence summary In Chlamydomonas, the pyrenoid-localized bestrophin-like protein BST4 is a putative ion channel involved in pH regulation of the thylakoid lumen, possibly by mediating bicarbonate transport