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Photosynthetic apparatus of Rhodobacter sphaeroides exhibits prolonged charge storage.

ABSTRACT: Photosynthetic proteins have been extensively researched for solar energy harvesting. Though the light-harvesting and charge-separation functions of these proteins have been studied in depth, their potential as charge storage systems has not been investigated to the best of our knowledge. Here, we report prolonged storage of electrical charge in multilayers of photoproteins isolated from Rhodobacter sphaeroides. Direct evidence for charge build-up within protein multilayers upon photoexcitation and external injection is obtained by Kelvin-probe and scanning-capacitance microscopies. Use of these proteins is key to realizing a 'self-charging biophotonic device' that not only harvests light and photo-generates charges but also stores them. In strong correlation with the microscopic evidence, the phenomenon of prolonged charge storage is also observed in primitive power cells constructed from the purple bacterial photoproteins. The proof-of-concept power cells generated a photovoltage as high as 0.45?V, and stored charge effectively for tens of minutes with a capacitance ranging from 0.1 to 0.2?F?m^-2.

SUBMITTER: Ravi SK

PROVIDER: S-EPMC6385238 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Photosynthetic apparatus of Rhodobacter sphaeroides exhibits prolonged charge storage.

Ravi Sai Kishore SK Rawding Piper P Elshahawy Abdelnaby M AM Huang Kevin K Sun Wanxin W Zhao Fangfang F Wang John J Jones Michael R MR Tan Swee Ching SC

Nature communications 20190222 1

Photosynthetic proteins have been extensively researched for solar energy harvesting. Though the light-harvesting and charge-separation functions of these proteins have been studied in depth, their potential as charge storage systems has not been investigated to the best of our knowledge. Here, we report prolonged storage of electrical charge in multilayers of photoproteins isolated from Rhodobacter sphaeroides. Direct evidence for charge build-up within protein multilayers upon photoexcitation ...[more]

PMID: 30796237

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Project description:ABSTRACT DksA is a global regulatory protein that, together with the alarmone ppGpp, is required for the "stringent response" to nutrient starvation in the gammaproteobacterium Escherichia coli and for more moderate shifts between growth conditions. DksA modulates the expression of hundreds of genes, directly or indirectly. Mutants lacking a DksA homolog exhibit pleiotropic phenotypes in other gammaproteobacteria as well. Here we analyzed the DksA homolog RSP2654 in the more distantly related Rhodobacter sphaeroides, an alphaproteobacterium. RSP2654 is 42% identical and similar in length to E. coli DksA but lacks the Zn finger motif of the E. coli DksA globular domain. Deletion of the RSP2654 gene results in defects in photosynthetic growth, impaired utilization of amino acids, and an increase in fatty acid content. RSP2654 complements the growth and regulatory defects of an E. coli strain lacking the dksA gene and modulates transcription in vitro with E. coli RNA polymerase (RNAP) similarly to E. coli DksA. RSP2654 reduces RNAP-promoter complex stability in vitro with RNAPs from E. coli or R. sphaeroides, alone and synergistically with ppGpp, suggesting that even though it has limited sequence identity to E. coli DksA (DksAEc), it functions in a mechanistically similar manner. We therefore designate the RSP2654 protein DksARsp. Our work suggests that DksARsp has distinct and important physiological roles in alphaproteobacteria and will be useful for understanding structure-function relationships in DksA and the mechanism of synergy between DksA and ppGpp. IMPORTANCE The role of DksA has been analyzed primarily in the gammaproteobacteria, in which it is best understood for its role in control of the synthesis of the translation apparatus and amino acid biosynthesis. Our work suggests that DksA plays distinct and important physiological roles in alphaproteobacteria, including the control of photosynthesis in Rhodobacter sphaeroides. The study of DksARsp, should be useful for understanding structure-function relationships in the protein, including those that play a role in the little-understood synergy between DksA and ppGpp.

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Photosynthetic apparatus of Rhodobacter sphaeroides exhibits prolonged charge storage.

Publications

Photosynthetic apparatus of Rhodobacter sphaeroides exhibits prolonged charge storage.

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