Engineering of B800 bacteriochlorophyll binding site specificity in the Rhodobacter sphaeroides LH2 antenna

Swainsbury, David J. K.; Faries, Kaitlyn M.; Niedzwiedzki, Dariusz M.; Martin, Elizabeth C.; Flinders, Adam J.; Canniffe, Daniel P.; Shen, Gaozhong; Bryant, Donald A.; Kirmaier, Christine; Holten, Dewey; Hunter, C. Neil

doi:10.1016/j.bbabio.2018.11.008

Title: Engineering of B800 bacteriochlorophyll binding site specificity in the Rhodobacter sphaeroides LH2 antenna

Journal Article · Fri Nov 09 00:00:00 EST 2018 · Biochimica et Biophysica Acta - Bioenergetics

DOI:https://doi.org/10.1016/j.bbabio.2018.11.008· OSTI ID:1482755

Swainsbury, David J. K.; Faries, Kaitlyn M.; Niedzwiedzki, Dariusz M.; Martin, Elizabeth C.; Flinders, Adam J.; Canniffe, Daniel P.;

; Bryant, Donald A.;

;

; Hunter, C. Neil

The light-harvesting 2 complex (LH2) of the purple phototrophic bacterium Rhodobacter sphaeroides is a highly efficient, light-harvesting antenna that allows growth under a wide-range of light intensities. In order to expand the spectral range of this antenna complex, we first used a series of competition assays to measure the capacity of the non-native pigments 3-acetyl chlorophyll (Chl) a, Chl d, Chl f or bacteriochlorophyll (BChl) b to replace native BChl a in the B800 binding site of LH2. We then adjusted the B800 site and systematically assessed the binding of non-native pigments. We find that Arg_–10 of the LH2 β polypeptide plays a crucial role in binding specificity, by providing a hydrogen-bond to the 3-acetyl group of native and non-native pigments. Reconstituted LH2 complexes harbouring the series of (B)Chls were examined by transient absorption and steady-state fluorescence spectroscopies. Although slowed 10-fold to ~6 ps, energy transfer from Chl a to B850 BChl a remained highly efficient. We measured faster energy-transfer time constants for Chl d (3.5 ps) and Chl f (2.7 ps), which have red-shifted absorption maxima compared to Chl a. BChl b, red-shifted from the native BChl a, gave extremely rapid (≤0.1 ps) transfer. These results show that modified LH2 complexes, combined with engineered (B)Chl biosynthesis pathways in vivo, have potential for retaining high efficiency whilst acquiring increased spectral range.

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Research Organization:: Energy Frontier Research Centers (EFRC) (United States). Photosynthetic Antenna Research Center (PARC); Pennsylvania State Univ., University Park, PA (United States); Washington Univ., St. Louis, MO (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences, and Biosciences Division; Biotechnology and Biological Sciences Research Council (BBSRC); National Science Foundation (NSF); European Commission Marie Skłodowska-Curie Global Fellowship

Grant/Contract Number:: SC0001035; FG02-94ER20137; BB/M000265/1

OSTI ID:: 1482755

Alternate ID(s):: OSTI ID: 1566431

Journal Information:: Biochimica et Biophysica Acta - Bioenergetics, Journal Name: Biochimica et Biophysica Acta - Bioenergetics Vol. 1860 Journal Issue: 3; ISSN 0005-2728

Publisher:: ElsevierCopyright Statement

Country of Publication:: Netherlands

Language:: English

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Cited by: 29 works

Citation information provided by
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59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
solar (fuels)
photosynthesis (natural and artificial)
biofuels (including algae and biomass)
bio-inspired
charge transport
membrane
synthesis (novel materials)
synthesis (self-assembly)
Rhodobacter sphaeroides
LH2
bacteriochlorophyll
chlorophyll
light harvesting
ligand binding
protein engineering

Title: Engineering of B800 bacteriochlorophyll binding site specificity in the Rhodobacter sphaeroides LH2 antenna

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