Dynamical Decoupling of Qubits in Spin Bath under Periodic Quantum Control

We investigate the feasibility for the preservation of coherence and entanglement of one and two spin qubits coupled to an interacting quantum spin-1/2 chain within the dynamical decoupling (DD) scheme. The performance is examined by counting number of computing pulses that can be applied periodically with period of $T$ before qubits become decoherent, while identical decoupling pulse sequence is applied within each cycle. By considering pulses with mixed directions and finite width controlled by magnetic fields, it is shown that pulse-width accumulation degrades the performance of sequences with larger number of pulses and feasible magnetic fields in practice restrict the consideration to sequences with number of decoupling pulses being less than 10 within each cycle. Furthermore, within each cycle $T$, exact nontrivial pulse sequences are found for the first time to suppress the qubit-bath coupling to $O(T^{N+1})$ progressively with minimum number of pulses being $4,7,12$ for $N=1,2,3$. These sequences, when applied to all qubits, are shown to preserve both the entanglement and coherence. Based on time-dependent density matrix renormalization, our numerical results show that for modest magnetic fields (10-40 Tesla) available in laboratories, the overall performance is optimized when number of pulses in each cycle is 4 or 7 with pulse directions be alternating between x and z. Our results provide useful guides for the preservation of coherence and entanglement of spin qubits in solid state.Comment: 11 pages, 9 figure

The Arabidopsis thiamin-deficient mutant pale green1 lacks thiamin monophosphate phosphatase of the vitamin B1 biosynthesis pathway

Thiamin diphosphate (TPP, vitamin B-1) is an essential coenzyme present in all organisms. Animals obtain TPP from their diets, but plants synthesize TPPde novo. We isolated and characterized an Arabidopsis pale green1 (pale1) mutant that contained higher concentrations of thiamin monophosphate (TMP) and less thiamin and TPP than the wild type. Supplementation with thiamin, but not the thiazole and pyrimidine precursors, rescued the mutant phenotype, indicating that the pale1 mutant is a thiamin-deficient mutant. Map-based cloning and whole-genome sequencing revealed that the pale1 mutant has a mutation in At5g32470 encoding a TMP phosphatase of the TPP biosynthesis pathway. We further confirmed that the mutation of At5g32470 is responsible for the mutant phenotypes by complementing the pale1 mutant with constructs overexpressing full-length At5g32470. Most plant TPP biosynthetic enzymes are located in the chloroplasts and cytosol, but At5g32470-GFP localized to the mitochondrion of the root, hypocotyl, mesophyll and guard cells of the 35S:At5g32470-GFP complemented plants. The subcellular localization of a functional TMP phosphatase suggests that the complete vitamin B1 biosynthesis pathway may involve the chloroplasts, mitochondria and cytosol in plants. Analysis of PALE1 promoter-uidA activity revealed that PALE1 is mainly expressed in vascular tissues of Arabidopsis seedlings. Quantitative RT-PCR analysis of TPP biosynthesis genes and genes encoding the TPP-dependent enzymes pyruvate dehydrogenase, -ketoglutarate dehydrogenase and transketolase revealed that the transcript levels of these genes were upregulated in the pale1 mutant. These results suggest that endogenous levels of TPP may affect the expression of genes involved in TPP biosynthesis and TPP-dependent enzymes