Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123

Volume: 1857, Issue: 9, Pages: 1490 - 1496
Published: Sep 1, 2016
Abstract
Resonance Raman spectroscopy was used to evaluate the structure of light-harvesting chlorophyll (Chl) a/b complexes of photosystem II (LHCII), reconstituted from wild-type (WT) and mutant apoproteins over-expressed in Escherichia coli. The point mutations involved residue S123, exchanged for either P (S123P) or G (S123G). In all reconstituted proteins, lutein 2 displayed a distorted conformation, as it does in purified LHCII trimers....
Paper Details
Title
Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123
Published Date
Sep 1, 2016
Volume
1857
Issue
9
Pages
1490 - 1496
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