Recombinant Aneura mirabilis Photosystem Q (B) protein
Description
Overview of Recombinant Aneura mirabilis Photosystem Q(B) Protein
Recombinant Aneura mirabilis Photosystem Q(B) protein refers to the engineered version of the Photosystem II (PSII) D1 protein (PsbA) from the parasitic liverwort Aneura mirabilis. This protein is critical for light-driven electron transport in PSII, though Aneura mirabilis itself has lost most photosynthetic functionality due to its parasitic lifestyle . The recombinant form is expressed in E. coli with an N-terminal His tag for purification and structural/functional studies .
Functional Significance in Photosynthesis
The D1 protein (PsbA) is central to PSII’s light-dependent reactions:
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Electron Transfer: The Q(B) site binds plastoquinone (PQ), enabling sequential oxidation of water and reduction of PQ .
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Protein Stability: Interactions with assembly factors (e.g., CtpA, CPRabA5e) ensure proper C-terminal processing and integration into PSII complexes .
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Herbicide Target: The Q(B) pocket is a binding site for PSII-inhibiting herbicides like terbutryn, which block electron transfer .
Production Parameters
Research Applications
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Structural Biology: Studying PSII supercomplex assembly and quinone binding dynamics .
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Evolutionary Studies: Investigating gene loss in parasitic plants (e.g., Aneura mirabilis) .
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Drug Development: Testing herbicide interactions with conserved Q(B) residues .
Key Discoveries
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Conservation of Q(B) Site: Structural studies of cyanobacterial PSII reveal high conservation of Q(B) residues (e.g., His215, Ser264) across oxygenic phototrophs, including A. mirabilis .
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Assembly Dependencies: Proteases like CtpA2 are essential for D1 C-terminal processing, a step critical for PSII maturation .
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Parasitism and Gene Loss: Aneura mirabilis retains psbA but has lost other photosynthetic genes (e.g., petA, petB), highlighting relaxed selection on non-essential PSII components .
Emerging Questions
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How does the recombinant D1 protein from A. mirabilis differ functionally from active PSII proteins in phototrophs?
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What structural insights into Q(B) binding can be derived from comparative studies of A. mirabilis and Prorocentrum micans PsbA?
Product Specs
Note: We will prioritize shipping the format currently in stock. However, if you have specific requirements for the format, please indicate them in your order remarks, and we will prepare according to your request.
Note: All our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please inform us in advance as additional fees will apply.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
