Ru–protein–Co biohybrids designed for solar hydrogen production: understanding electron transfer pathways related to photocatalytic function

Soltau, Sarah R.; Dahlberg, Peter D.; Niklas, Jens; Poluektov, Oleg G.; Mulfort, Karen L.; Utschig, Lisa M.

doi:10.1039/c6sc03121h

Cited by 32 publications

(43 citation statements)

References 69 publications

(102 reference statements)

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“…To increase enzymatic efficiency, the multi-molecular systems are required to be integrated in a single system such as protein-based system for facilitating electron transfer [203]. Recently, Utschig and coworkers [204] designed a series of Ru-protein-Co biohybrids for photocatalytic H2 production, by directly linking both the photosensitizer, [Ru(bpy)3] 2+ , and the catalyst, Co(dmgH)2pyCl (CoPy) or Co(dmgBF2)2•H2O (CoBF2) (Fig. 32a), to the an electron transfer protein, ferredoxin (Fd) (Fig.…”

Section: In Single Protein Scaffoldsmentioning

confidence: 99%

“…Fourth, the design is moving from simple to complex systems. Although the majority of successful designs are focused on simple models mimicking the active center of natural enzymes, some efforts have been made to design of more complex systems, such as membrane systems [48,49], photocatalytic systems [204,229] and multi-enzyme systems [230][231][232]. These achievements represent the major breakthrough in protein design, and more efforts need to be made in this field, which will bring us closer to the success in mimicking the native systems.…”

Section: Conclusion and Perspectivementioning

confidence: 99%

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Rational design of metalloenzymes: From single to multiple active sites

Lin

2017

Coordination Chemistry Reviews

130

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Artificial metalloenzymes combine the advantages of both natural enzymes and chemically synthesized models, which have achieved significant progress in the last decade. This review summarizes the recent achievements in rational design of metalloenzymes from single to multiple active sites in natural or de novo protein scaffolds, with a diverse range of functionalities, even beyond those of natural metalloenzymes. These achievements include construction of mononuclear active site by metal substitution or incorporation, design of homo-or hetero-dinuclear site, introduction of Fe-sulfur or other metal clusters, reconstitution of metallo-porphyrins or other metal complexes, and design of dual or multiple active sites in single, dimeric proteins, de novo proteins, protein-protein interfaces, as well as protein oligomers and polymers. Other new trends in recent designs are also discussed. The progress not only elucidates the structural and functional relationship of natural metalloenzymes, but also provides practical clues for design of advanced artificial metalloenzymes with potential applications.

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Section: In Single Protein Scaffoldsmentioning

confidence: 99%

Section: Conclusion and Perspectivementioning

confidence: 99%

Rational design of metalloenzymes: From single to multiple active sites

Lin

2017

Coordination Chemistry Reviews

130

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“…Their oxygen sensitivity and production costs call for the development of artificial hydrogenases. Several artificial hydrogenases rely on the incorporation of artificial metal cofactors in host proteins (cytochrome c , rubredoxin, ferredoxin) or linking to a polypeptide . In the past decade, the biotin‐streptavidin technology has found widespread use for the assembly of artificial metalloenzymes (ArM) .…”

Section: Introductionmentioning

confidence: 99%

Photo‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology

Keller

Probst

Heinisch

et al. 2018

Helvetica Chimica Acta

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Photocatalytic hydrogen evolution by an artificial hydrogenase based on the biotin‐streptavidin technology is reported. A biotinylated cobalt pentapyridyl‐based hydrogen evolution catalyst (HEC) was incorporated into different mutants of streptavidin. Catalysis with [Ru(bpy)3]Cl2 as a photosensitizer (PS) and ascorbate as sacrificial electron donor (SED) at different pH values highlighted the impact of close lying amino acids that may act as a proton relay under the reaction conditions (Asp, Arg, Lys). In the presence of a close‐lying lysine residue, both, the rates were improved, and the reaction was initiated much faster. The X‐ray crystal structure of the artificial hydrogenase reveals a distance of 8.8 Å between the closest lying Co‐moieties. We thus suggest that the hydrogen evolution mechanism proceeds via a single Co centre. Our findings highlight that streptavidin is a versatile host protein for the assembly of artificial hydrogenases and their activity can be fine‐tuned via mutagenesis.

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“…Transient absorption data for BiotH2 were satisfactorily fitted with 4 lifetimes: 17 ns, 10 μs, 51 μs and 486 μs. The EADS corresponding to the species with a 17 ns lifetime shows broad induced absorption at 500–800 nm and ground state bleaching at 450 nm characteristic of the [Ru(Bpy) 3 ] 2+ excited state . This state decays via an electron transfer from the ascorbic acid to form the transient [Ru(Bpy) 3 ] + species, which has a characteristic strong induced absorption at 520 nm .…”

Section: Resultsmentioning

confidence: 99%

“…Compared to the hydrogenases, these models show moderate catalytic activity, and generally are inefficient catalysts in photoinduced hydrogen production in part because they degrade during long irradiation, often resulting in the loss of the CO ligands . Simple diiron‐dithiolate complexes have also been encased within biopolymers or non‐biological scaffolds, such as cyclodextrins, surfactants, dendrimers, or metal‐organic frameworks (MOFs), showing that supramolecular confinement enhances photoinduced hydrogen production . However, these systems cannot provide the tailored second‐sphere interactions that in natural hydrogenases activate the organometallic center by stabilization of the catalytically active conformation …”

Section: Introductionmentioning

confidence: 99%

Enhanced Photocatalytic Hydrogen Production by Hybrid Streptavidin‐Diiron Catalysts

Vaughn

Tomlin

Booher

et al. 2020

Chemistry A European J

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Hybrid protein–organometallic catalysts are being explored for selective catalysis of a number of reactions, because they utilize the complementary strengths of proteins and of organometallic complex. Herein, we present an artificial hydrogenase, StrepH2, built by incorporating a biotinylated [Fe–Fe] hydrogenase organometallic mimic within streptavidin. This strategy takes advantage of the remarkable strength and specificity of biotin‐streptavidin recognition, which drives quantitative incorporation of the biotinylated diironhexacarbonyl center into streptavidin, as confirmed by UV/Vis spectroscopy and X‐ray crystallography. FTIR spectra of StrepH2 show characteristic peaks at shift values indicative of interactions between the catalyst and the protein scaffold. StrepH2 catalyzes proton reduction to hydrogen in aqueous media during photo‐ and electrocatalysis. Under photocatalytic conditions, the protein‐embedded catalyst shows enhanced efficiency and prolonged activity compared to the isolated catalyst. Transient absorption spectroscopy data suggest a mechanism for the observed increase in activity underpinned by an observed longer lifetime for the catalytic species FeIFe0 when incorporated within streptavidin compared to the biotinylated catalyst in solution.

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Ru–protein–Co biohybrids designed for solar hydrogen production: understanding electron transfer pathways related to photocatalytic function

Abstract: Two ruthenium-protein-cobaloxime biohybrids produce photocatalytic hydrogen through different catalytic pathways characterized by EPR and transient optical spectroscopies.

Cited by 32 publications

References 69 publications

Rational design of metalloenzymes: From single to multiple active sites

Rational design of metalloenzymes: From single to multiple active sites

Photo‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology

Enhanced Photocatalytic Hydrogen Production by Hybrid Streptavidin‐Diiron Catalysts

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