Abstract
CHLOROPHYLL (Chl), in vivo as well as in protein complexes purified from photosynthetic organisms, absorbs light at longer wavelengths than does Chl as an isolated molecule in an organic solvent1. These bathochromic absorbance shifts are substantial, up to 40 nm (800 cm−1) for Chl a in green plants and 100 nm (1,400 cm−1) for bacteriochlorophyll (Bchl) a in photosynthetic bacteria. An important question is whether these shifts are caused largely by Chl–Chl interactions or by interactions between Chl and the proteins to which all Chl is bound in vivo2–4. This has been difficult to answer because no native Chl–protein complex yet found contains only one pigment molecule. We report here, substituting the water-soluble Chl derivative, chlorophyllin (Chln) a, for haem in myoglobin, and irradiating the resultant complex with red light, the first model Chl–protein complex that verifiably contains a single pigment molecule and that also exhibits a 1,000 cm−1 bathochromic shift in absorbance.
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DAVIS, R., PEARLSTEIN, R. Chlorophyllin–apomyoglobin complexes. Nature 280, 413–415 (1979). https://doi.org/10.1038/280413a0
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DOI: https://doi.org/10.1038/280413a0
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