Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy

Jiang, Xiue; Zaitseva, Ekaterina; Schmidt, Matthias R.; Siebert, Friedrich; Engelhard, Martin; Schlesinger, Ramona; Ataka, Kenichi; Vogel, Reiner; Heberle, Joachim

doi:10.1073/pnas.0802289105

Cited by 131 publications

(173 citation statements)

References 37 publications

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Section: Spectroscopiesmentioning

confidence: 99%

“…For β-sheets, the situation is reversed for the main amide I and amide II components. As a consequence of this surface selection rule, the intensity ratio between Amide I and Amide II bands brings information regarding the orientation of the enzyme provided that a structure or a model of the enzyme is available [148] (Figure 8). Surface-Enhanced Infrared Absorption (SEIRA) spectroscopy was used in combination with MD simulations to observe and rationalize the immobilization in a controlled orientation of membranebound [NiFe]-Hase from Ralstonia eutropha [149].…”

Section: Spectroscopiesmentioning

confidence: 99%

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Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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Abstract:Redox enzymes, which catalyze reactions involving electron transfers in living organisms, are very promising components of biotechnological devices, and can be envisioned for sensing applications as well as for energy conversion. In this context, one of the most significant challenges is to achieve efficient direct electron transfer by tunneling between enzymes and conductive surfaces. Based on various examples of bioelectrochemical studies described in the recent literature, this review discusses the issue of enzyme immobilization at planar electrode interfaces. The fundamental importance of controlling enzyme orientation, how to obtain such orientation, and how it can be verified experimentally or by modeling are the three main directions explored. Since redox enzymes are sizable proteins with anisotropic properties, achieving their functional immobilization requires a specific and controlled orientation on the electrode surface. All the factors influenced by this orientation are described, ranging from electronic conductivity to efficiency of substrate supply. The specificities of the enzymatic molecule, surface properties, and dipole moment, which in turn influence the orientation, are introduced. Various ways of ensuring functional immobilization through tuning of both the enzyme and the electrode surface are then described. Finally, the review deals with analytical techniques that have enabled characterization and quantification of successful achievement of the desired orientation. The rich contributions of electrochemistry, spectroscopy (especially infrared spectroscopy), modeling, and microscopy are featured, along with their limitations.

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Section: Spectroscopiesmentioning

confidence: 99%

Section: Spectroscopiesmentioning

confidence: 99%

Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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“…Since electron transfer is direct and there is no dependence on diffusion of either mediators or the protein of interest, the SEIRA approach is suited to time-resolved rapid-scan (seconds) or step-scan (milliseconds) methods. Orientation-selective attachment of proteins to the gold surface is advantageous for homogeneity in the film and efficient electron transfer, and Jiang et al (2008) and others have made use of SAMs capped with a nickel nitriloacetic acid complex to selectively coordinate poly-histidine of 'His-tagged' proteins (figure 6b).…”

Section: (C) Electrochemical Triggers (Spectroelectrochemistry )mentioning

confidence: 99%

Triggered infrared spectroscopy for investigating metalloprotein chemistry

Vincent

2010

Phil. Trans. R. Soc. A.

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Recent developments in infrared (IR) spectroscopic time resolution, sensitivity and sample manipulation make this technique a powerful addition to the suite of complementary approaches for the study of time-resolved chemistry at metal centres within proteins. Application of IR spectroscopy to proteins has often targeted the amide bands as probes for gross structural change. This article focuses on the possibilities arising from recent IR technical developments for studies that monitor localized vibrational oscillators in proteins-native or exogenous ligands such as NO, CO, SCN − or CN − , or genetically or chemically introduced probes with IR-active vibrations. These report on the electronic and coordination state of metals, the kinetics, intermediates and reaction pathways of ligand release, hydrogen-bonding interactions between the protein and IR probe, and the electrostatic character of sites in a protein. Metalloprotein reactions can be triggered by light/dark transitions, an electrochemical step, a change in solute composition or equilibration with a new gas atmosphere, and spectra can be obtained over a range of time domains as far as the sub-picosecond level. We can expect to see IR spectroscopy exploited, alongside other spectroscopies, and crystallography, to elucidate reactions of a wide range of metalloprotein chemistry with relevance to cell metabolism, health and energy catalysis.

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“…Heberle's group studied the Sensory rhodopsin II (SR II) immobilized on a gold surface [77,78]. SR II is the primary light sensor for negative phototaxis, which can be activated by bluegreen light to its transducer protein Htr II.…”

Section: The Artificial Membrane Systemmentioning

confidence: 99%

“…One route is to immobilize tethered membrane protein on a surface and then reconstitute the lipid bilayer around the protein by detergent-lipid exchange (Fig. 6a) [75][76][77][78][79]. Usually, the protein is recombined with an oligo-histidine tag (His-tag) by genetic engineering, offering more stable and specific adsorption on the surface with di-covalent ions via chelators such as nitrilotriacetic acid (NTA).…”

Section: The Artificial Membrane Systemmentioning

confidence: 99%

Attenuated Total Reflection Surface-Enhanced Infrared Absorption Spectroscopy: a Powerful Technique for Bioanalysis

Zhang

et al. 2017

J. Anal. Test.

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Attenuated total reflection surface-enhanced infrared absorption spectroscopy (ATR-SEIRAS) has recently been proven to be a powerful tool for bioanalysis. It enables in situ and in real-time observation of dynamic processes occurring on specific interface, revealing rich structural and functional information of biomolecules at sub monolayer level. The aim of this general review was to give an overview of the cutting edge applications of ATR-SEIRAS. We start with description of the basic configuration of the standard ATR-SEIRAS platform. The enhanced mechanisms and methods to fabricate enhanced substrates are then presented. We discuss the recent developments, challenges and applications of ATR-SEIRAS in bioanalysis, mainly focusing on DNA analysis, protein behavior and cell properties. Finally, further development of the ATR-SEIRAS technique with enhanced sensitivity, improved time and spatial resolutions will be prospected.

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Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy

Cited by 131 publications

References 37 publications

Controlling Redox Enzyme Orientation at Planar Electrodes

Controlling Redox Enzyme Orientation at Planar Electrodes

Triggered infrared spectroscopy for investigating metalloprotein chemistry

Attenuated Total Reflection Surface-Enhanced Infrared Absorption Spectroscopy: a Powerful Technique for Bioanalysis

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