Publications by authors named "Ya-Fang Sun"

To improve the effectiveness of government environmental attention on resource allocation, this study proposes a measurement framework using text analysis and an unsupervised Word2vec model to quantify local government environmental attention of 288 Chinese cities. We further examine its impact on total factor productivity (TFP) of China's listed firms from 2010 to 2021 using the high-dimensional fixed-effects and panel quantile regression models. The findings show that: (1) Local government environmental attention contributes positively to TFP, with each unit increase raising TFP by approximately 1.

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Economic sectors are pivotal in achieving China's dual carbon goals; nevertheless, the combined impact of industrial and energy consumption structures on sectors' peak pathways remains unresolved. We extend the optimization of separate industrial and energy structures to a multi-objective dynamic input-output optimization model. Findings indicate the following.

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The transport sector proves a major energy consumer in China, but improving energy-saving performance in China's provincial transport sector from the lifecycle perspective remains unresolved. Thus, this study employs the environmentally extended multi-region input-output (MRIO) method, structural path analysis, and the newest MRIO table of China from 2017, to investigate how to improve the energy-saving performance from final demand structure, supply chain, and pathway perspectives. The relevant results are threefold.

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Cyanobacteriochromes (CBCRs) are photochromic proteins in cyanobacteria that act as photosensors. CBCRs bind bilins as chromophores and sense nearly the entire visible spectrum of light, but the regulation of the chromophorylation of CBCRs is unknown. Slr1393 from sp.

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Validamycin A (Val-A) is produced by Streptomyces as a secondary metabolite with wide agricultural applications of controlling rice sheath blight, false smut and damping-off diseases. The effect of alkaline pH shock on enhancing Val-A production and its mechanism were investigated. A higher yield of Val-A was achieved by NaOH shock once or several times together with faster protein synthesis and sugar consumption and alkaline pH shock can increase Val-A production by 27.

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Cyanobacteria are among the main contributors to global photosynthesis and show a high degree of metabolic plasticity. Synechocystis sp. PCC 6803 can grow under photoautotrophic, photomixotrophic or photoheterotrophic conditions.

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Allophycocyanin B (AP-B) is one of the two terminal emitters in phycobilisomes, the unique light-harvesting complexes of cyanobacteria and red algae. Its low excitation-energy level and the correspondingly redshifted absorption and fluorescence emission play an important role in funnelling excitation energy from the hundreds of chromophores of the extramembraneous phycobilisome to the reaction centres within the photosynthetic membrane. In the absence of crystal structures of these low-abundance terminal emitters, the molecular basis for the extreme redshift and directional energy transfer is largely unknown.

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Cyanobacteriochromes are a structurally and spectrally highly diverse class of phytochrome-related photosensory biliproteins. They contain one or more GAF domains that bind phycocyanobilin (PCB) autocatalytically; some of these proteins are also capable of further modifying PCB to phycoviolobilin or rubins. We tested the chromophorylation with the non-photochromic phycoerythrobilin (PEB) of 16 cyanobacteriochrome GAFs from Nostoc sp.

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The phycocyanin lyase CpcT1 (encoded by gene all5339) and lyase CpcS1 (encoded by gene alr0617) are capable of catalyzing the phycocyanobilin (PCB) covalently bound to the different sites of phycocyanin's and phycoerythrocyanin's β subunits, respectively. Lyase CpcS1, whose catalytic mechanism had been researched clearly, participates in the covalent coupling of phycobilin and apoprotein in the form of chaperone, and its important amino acids have been confirmed. In order to identify the functional amino acid residues of CpcT1, chemical modification was conducted to arginine, histidine, tryptophan, lysine and amino acid carboxyl of CpcT1.

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