Wiley, FEBS Letters, 1-2(491), p. 143-147, 2001
DOI: 10.1016/s0014-5793(01)02161-5
Full text: Unavailable
In this work we have selectively released the 800 nm absorbing bacteriochlorophyll a molecules of the LH2 protein from the photosynthetic bacterium Rhodopseudomonas acidophila, strain 10050, and replaced them with chlorophyll a (Chla). A combination of low-temperature electronic absorption, resonance Raman and site-selection fluorescence spectroscopies revealed that the Chla pigments are indeed bound in the B800 binding site; this is the first work that formally proves that such non-native chlorins can be inserted correctly into LH2.