Bioelectronic Circuit on a 3D Electrode Architecture: Enzymatic Catalysis Interconnected with Photosystem I

Ciornii, Dmitri; Riedel, Marc; Stieger, Kai Ralf; Feifel, Sven C.; Hejazi, Mahdi; Lokstein, Heiko; Zouni, Athina; Lisdat, Fred

doi:10.1021/jacs.7b10161

Cited by 52 publications

(60 citation statements)

References 30 publications

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“…31 Using 2D IR and isotope labeling, our group has demonstrated the presence of a transient β -sheet in amylin that is ultimately part of a disordered loop in the fiber. 32–34 Thus, it appears that oligomers of amyloidogenic proteins may often adopt a different structure than that of the amyloid fibril. In this study, we find that we can exploit the differences in β -sheet sheet structure, even in the absence of isotope labels, to distinguish β -sheet-rich A β oligomers from A β fibrils.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers

et al. 2017

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We use two-dimensional IR (2D IR) spectroscopy to explore fibril formation for the two predominant isoforms of the β-amyloid (Aβ1–40 and Aβ1–42) protein associated with Alzheimer’s disease. Two-dimensional IR spectra resolve a transition at 1610 cm−1 in Aβ fibrils that does not appear in other Aβ aggregates, even those with predominantly β-sheet-structure-like oligomers. This transition is not resolved in linear IR spectroscopy because it lies under the broad band centered at 1625 cm−1, which is the traditional infrared signature for amyloid fibrils. The feature is prominent in 2D IR spectra because 2D lineshapes are narrower and scale nonlinearly with transition dipole strengths. Transmission electron microscopy measurements demonstrate that the 1610 cm−1 band is a positive identification of amyloid fibrils. Sodium dodecyl sulfate micelles that solubilize and disaggregate preaggregated Aβ samples deplete the 1625 cm 1 band but do not affect the 1610 cm 1 band, demonstrating that the 1610 cm−1 band is due to very stable fibrils. We demonstrate that the 1610 cm−1 transition arises from amide I modes by mutating out the only side-chain residue that could give rise to this transition, and we explore the potential structural origins of the transition by simulating 2D IR spectra based on Aβ crystal structures. It was not previously possible to distinguish stable Aβ fibrils from the less stable β-sheet-rich oligomers with infrared light. This 2D IR signature will be useful for Alzheimer’s research on Aβ aggregation, fibril formation, and toxicity.

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Section: Introductionmentioning

confidence: 99%

Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers

et al. 2017

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“…This device is capable of yielding a light‐to‐hydrogen conversion efficiency of as much as 5.4 % . Alternatively, using photosystem I, cytochrome c and human sulfite oxidase, Lisdat and co‐workers have demonstrated the possibility of using ITO as a support for light‐driven bio‐sensing redox enzyme devices …”

Section: Carbon Electrodesmentioning

confidence: 99%

“…[84] Alternatively,u sing photosystem I, cytochromec and human sulfite oxidase, Lisdat and co-workers have demonstrated the possibility of using ITO as as upport for light-driven bio-sensing redox enzymedevices. [94] As with PGE, nonspecific adsorption of protein to as emiconductor can be facilitated by considering the effect of pH. For example, the isoelectricp oint (pI) of aT iO 2 surface was found to be 6.2, [95] whereas the pI values of ac arbon monoxide dehydrogenase [96] and a[ NiFeSe]-hydrogenase [83] were found to be 5.5 and5 .4, respectively.B oth enzymes could be adsorbed to TiO 2 nanoparticlesa tp H6, [83,97,98] and this has been rationalized by considering that under these conditions the net surface chargeo ft he enzymes is negative whereas that of the TiO 2 is positive.…”

Section: Metal Oxide Semiconductorsmentioning

confidence: 99%

Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces

Yates

Fascione

Parkin

2018

Chemistry A European J

109

116

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The immobilization of redox proteins or enzymes onto conductive surfaces has application in the analysis of biological processes, the fabrication of biosensors, and in the development of green technologies and biochemical synthetic approaches. This review evaluates the methods through which redox proteins can be attached to electrode surfaces in a “wired” configuration, that is, one that facilitates direct electron transfer. The feasibility of simple electroactive adsorption onto a range of electrode surfaces is illustrated, with a highlight on the recent advances that have been achieved in biotechnological device construction using carbon materials and metal oxides. The covalent crosslinking strategies commonly used for the modification and biofunctionalization of electrode surfaces are also evaluated. Recent innovations in harnessing chemical biology methods for electrically wiring redox biology to surfaces are emphasized.

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“…[11,12] Three-dimensional electrodes offer another avenue for increasing the areal protein loading. [14,18,[28][29][30][31][32][33] Ciesielski et al…”

Section: Introductionmentioning

confidence: 99%

Photosystem I Multilayers within Porous Indium Tin Oxide Cathodes Enhance Mediated Electron Transfer

et al. 2019

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Understanding and improving charge transfer pathways between extracted Photosystem I (PSI) protein complexes and electrodes is necessary for the development of low‐cost PSI‐based devices for energy conversion. We incorporated PSI multilayers within porous indium tin oxide (ITO) electrodes and observed a greater mediated photocurrent in comparison to multilayers on planar ITO. First, the mediated electron transfer (MET) pathway in the presence of 2,6‐dichlorophenolindophenol (DCPIP) and ascorbate (AscH) was studied via photochronoamperometry on planar ITO. ITO nanoparticles were then used to fabricate two porous electrode morphologies; mesoporous (20–100 nm pores) and macroporous (5 μm pores). PSI multilayers within macroporous ITO cathodes produced 42±5 μA cm−2 of photocurrent, three times the photocurrent produced by mesoporous ITO. Additionally, macroporous cathodes are able to utilize twice as much active surface area, when compared to mesoporous cathodes. Our findings show that MET within PSI multilayers is greater in 5 μm macropores than mesoporous ITO due to both an increase in electrode surface area and the location of PSI complexes within the pores. Improving MET in PSI‐based bioelectrodes has applications including improving the total charge transfer achieved in PSI‐based photoelectrochemical cells or even incorporation in bio‐photocatalytic cells.

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Bioelectronic Circuit on a 3D Electrode Architecture: Enzymatic Catalysis Interconnected with Photosystem I

Cited by 52 publications

References 30 publications

Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers

Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers

Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces

Photosystem I Multilayers within Porous Indium Tin Oxide Cathodes Enhance Mediated Electron Transfer

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