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• W2073973503 abstract "The central photochemical reaction in photosystem II of green algae and plants and the reaction center of some photosynthetic bacteria involves a one-electron transfer from a light-activated chlorin complex to a bound quinone molecule. Through protein engineering, we have been able to modify a protein to mimic this reaction. A unique quinone-binding site was engineered into the Escherichia coli cytochrome b 562 by introducing a cysteine within the hydrophobic interior of the protein. Various quinones, such as p -benzoquinone and 2,3-dimethoxy-5-methyl-1,4-benzoquinone, were then covalently attached to the protein through a cysteine sulfur addition reaction to the quinone ring. The cysteine placement was designed to bind the quinone ≈10 Å from the edge of the bound porphyrin. Fluorescence measurements confirmed that the bound hydroquinone is incorporated toward the protein's hydrophobic interior and is partially solvent-shielded. The bound quinones remain redox-active and can be oxidized and rereduced in a two-electron process at neutral pH. The semiquinone can be generated at high pH by a one-electron reduction, and the midpoint potential of this can be adjusted by ≈500 mV by binding different quinones to the protein. The heme-binding site of the modified cytochrome was then reconstituted with the chlorophyll analogue zinc chlorin e 6 . By using EPR and fast optical techniques, we show that, in the various chlorin–protein–quinone complexes, light-induced electron transfer can occur from the chlorin to the bound oxidized quinone but not the hydroquinone, with electron transfer rates in the order of 10 8 s –1 ." @default.
• W2073973503 created "2016-06-24" @default.
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• W2073973503 date "2004-12-07" @default.
• W2073973503 modified "2023-10-03" @default.
• W2073973503 title "Protein engineering of cytochrome <i>b</i> ₅₆₂ for quinone binding and light-induced electron transfer" @default.
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• W2073973503 doi "https://doi.org/10.1073/pnas.0406192101" @default.
• W2073973503 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/539716" @default.
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