Dataset Information

Artificial Light-Harvesting Complexes Enable Rieske Oxygenase Catalyzed Hydroxylations in Non-Photosynthetic cells.

ABSTRACT: In this study, we coupled a well-established whole-cell system based on E.?coli via light-harvesting complexes to Rieske oxygenase (RO)-catalyzed hydroxylations in vivo. Although these enzymes represent very promising biocatalysts, their practical applicability is hampered by their dependency on NAD(P)H as well as their multicomponent nature and intrinsic instability in cell-free systems. In order to explore the boundaries of E.?coli as chassis for artificial photosynthesis, and due to the reported instability of ROs, we used these challenging enzymes as a model system. The light-driven approach relies on light-harvesting complexes such as eosin?Y, 5(6)-carboxyeosin, and rose bengal and sacrificial electron donors (EDTA, MOPS, and MES) that were easily taken up by the cells. The obtained product formations of up to 1.3?g?L-1 and rates of up to 1.6?mm?h-1 demonstrate that this is a comparable approach to typical whole-cell transformations in E.?coli. The applicability of this photocatalytic synthesis has been demonstrated and represents the first example of a photoinduced RO system.

SUBMITTER: Feyza Ozgen F

PROVIDER: S-EPMC7065155 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Artificial Light-Harvesting Complexes Enable Rieske Oxygenase Catalyzed Hydroxylations in Non-Photosynthetic cells.

Feyza Özgen F F Runda Michael E ME Burek Bastien O BO Wied Peter P Bloh Jonathan Z JZ Kourist Robert R Schmidt Sandy S

Angewandte Chemie (International ed. in English) 20200124 10

In this study, we coupled a well-established whole-cell system based on E. coli via light-harvesting complexes to Rieske oxygenase (RO)-catalyzed hydroxylations in vivo. Although these enzymes represent very promising biocatalysts, their practical applicability is hampered by their dependency on NAD(P)H as well as their multicomponent nature and intrinsic instability in cell-free systems. In order to explore the boundaries of E. coli as chassis for artificial photosynthesis, and due to the repor ...[more]

PMID: 31850622

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Project description:Chlorophototrophic organisms have a charge-separating reaction centre (RC) complex that receives energy from a dedicated light-harvesting (LH) antenna. In the purple phototrophic bacteria, these two functions are embodied by the 'core' photosynthetic component, the RC-LH1 complex. RC-LH1 complexes sit within a membrane bilayer, with the central RC wholly or partly surrounded by a curved array of LH1 subunits that bind a series of bacteriochlorophyll (BChl) and carotenoid pigments. Decades of research have shown that the absorption of light initiates a cascade of energy, electron, and proton transfers that culminate in the formation of a quinol, which is subsequently oxidized by the cytochrome bc1 complex. However, a full understanding of all these processes, from femtosecond absorption of light to millisecond quinone diffusion, requires a level of molecular detail that was lacking until the remarkable recent upsurge in the availability of RC-LH1 structures. Here, we survey 13 recently determined RC-LH1 assemblies, and we compare the precise molecular arrangements of pigments and proteins that allow efficient light absorption and the transfer of energy, electrons and protons. We highlight shared structural features, as well as differences that span the bound pigments and cofactors, the structures of individual subunits, the overall architecture of the complexes, and the roles of additional subunits newly identified in just one or a few species. We discuss RC-LH1 structures in the context of prior biochemical and spectroscopic investigations, which together enhance our understanding of the molecular mechanisms of photosynthesis in the purple phototrophic bacteria. A particular emphasis is placed on how the remarkable and unexpected structural diversity in RC-LH1 complexes demonstrates different evolutionary solutions for maximising pigment density for optimised light harvesting, whilst balancing the requirement for efficient quinone diffusion between RC and cytochrome bc1 complexes through the encircling LH1 complex.

Dataset Information

Artificial Light-Harvesting Complexes Enable Rieske Oxygenase Catalyzed Hydroxylations in Non-Photosynthetic cells.

Publications

Artificial Light-Harvesting Complexes Enable Rieske Oxygenase Catalyzed Hydroxylations in Non-Photosynthetic cells.

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