期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1861, 期 4, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bbabio.2019.148078
关键词
Chl-a; Hydrogen bonds; Light-harvesting; Energy regulation; Oxygenic photosynthesis
资金
- ERC funding agency (PHOTPROT project)
- French Infrastructure for Integrated Structural Biology (FRISBI) (France) [ANR-10-INBS-05]
- Dutch Organization for scientific research via TOP grant (Netherlands) [84713002]
- European Union [675006]
We describe a molecular mechanism tuning the functional properties of chlorophyll a (Chl-a) molecules in photosynthetic antenna proteins. Light-harvesting complexes from photosystem II in higher plants - specifically LHCII purified with alpha- or beta-dodecyl-maltoside, along with CP29 - were probed by low-temperature absorption and resonance Raman spectroscopies. We show that hydrogen bonding to the conjugated keto carbonyl group of protein-bound Chl-a tunes the energy of its Sorel and Q(y) absorption transitions, inducing red-shifts that are proportional to the strength of the hydrogen bond involved. Chls-a with non-H-bonded keto C13(1) groups exhibit the blue-most absorption bands, while both transitions are progressively red-shifted with increasing hydrogen-bonding strength - by up 382 & 605 cm(-1) in the Q(y) and Sorel band, respectively. These hydrogen bonds thus tune the site energy of Chl-a in light-harvesting proteins, determining (at least in part) the cascade of energy transfer events in these complexes.
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