SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes

Silveira, Célia M.; Quintas, Pedro O.; Moura, Isabel; Moura, José J. G.; Hildebrandt, Peter; Almeida, M. Gabriela; Todorović, Smilja

doi:10.1371/journal.pone.0129940

Cited by 15 publications

(43 citation statements)

References 46 publications

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“…59 For measurements, a laser line matching the electronic transition of the heme and concomitantly exciting the surface plasmons of a nanostructured Ag support is utilized. Stationary and time-resolved potential-controlled SERR spectroscopy have been applied to study the interfacial electron transfer of cyt c , 60 the communication between the heme cofactors in cytochrome c oxidase, 61 the heme cofactor of immobilized cytochrome P450, 62 the interaction between cytochrome cd 1 nitrite reductase and its physiological partner cytochrome c 552 on an electrode surface, 63 and the active site of a heme peroxidase 64 at biomimetically coated rough Ag electrodes. SERR spectroscopic investigations of the non-heme DNA-repairing enzyme endonuclease III revealed redox activity of the [4Fe–4S] cluster also in the absence of DNA-binding.…”

Section: Surface-enhanced Vibrational Spectroscopymentioning

confidence: 99%

Advancing Techniques for Investigating the Enzyme–Electrode Interface

Kornienko

Robinson

et al. 2019

Acc. Chem. Res.

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ConspectusEnzymes are the essential catalytic components of biology and adsorbing redox-active enzymes on electrode surfaces enables the direct probing of their function. Through standard electrochemical measurements, catalytic activity, reversibility and stability, potentials of redox-active cofactors, and interfacial electron transfer rates can be readily measured. Mechanistic investigations on the high electrocatalytic rates and selectivity of enzymes may yield inspiration for the design of synthetic molecular and heterogeneous electrocatalysts. Electrochemical investigations of enzymes also aid in our understanding of their activity within their biological environment and why they evolved in their present structure and function. However, the conventional array of electrochemical techniques (e.g., voltammetry and chronoamperometry) alone offers a limited picture of the enzyme–electrode interface.How many enzymes are loaded onto an electrode? In which orientation(s) are they bound? What fraction is active, and are single or multilayers formed? Does this static picture change over time, applied voltage, or chemical environment? How does charge transfer through various intraprotein cofactors contribute to the overall performance and catalytic bias? What is the distribution of individual enzyme activities within an ensemble of active protein films? These are central questions for the understanding of the enzyme–electrode interface, and a multidisciplinary approach is required to deliver insightful answers.Complementing standard electrochemical experiments with an orthogonal set of techniques has recently allowed to provide a more complete picture of enzyme–electrode systems. Within this framework, we first discuss a brief history of achievements and challenges in enzyme electrochemistry. We subsequently describe how the aforementioned challenges can be overcome by applying advanced electrochemical techniques, quartz-crystal microbalance measurements, and spectroscopic, namely, resonance Raman and infrared, analysis. For example, rotating ring disk electrochemistry permits the simultaneous determination of reaction kinetics and quantification of generated products. In addition, recording changes in frequency and dissipation in a quartz crystal microbalance allows to shed light into enzyme loading, relative orientation, clustering, and denaturation at the electrode surface. Resonance Raman spectroscopy yields information on ligation and redox state of enzyme cofactors, whereas infrared spectroscopy provides insights into active site states and the protein secondary and tertiary structure. The development of these emerging methods for the analysis of the enzyme–electrode interface is the primary focus of this Account. We also take a critical look at the remaining gaps in our understanding and challenges lying ahead toward attaining a complete mechanistic picture of the enzyme–electrode interface.

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Section: Surface-enhanced Vibrational Spectroscopymentioning

confidence: 99%

Advancing Techniques for Investigating the Enzyme–Electrode Interface

Kornienko

Robinson

et al. 2019

Acc. Chem. Res.

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“…Raman‐SEC has been successfully used in the study of redox‐active proteins immobilized on metallic substrates. The provided information is limited not only to faradaic processes, but it also provides simultaneous insight into structural and orientational parameters . The component analysis of the potential dependent SERS spectra of cytochrome c552 provides the relative spectral contributions of the ferric and ferrous heme c .…”

Section: Advantages In Usementioning

confidence: 99%

“…The provided information is limited not only to faradaic processes, but it also provides simultaneous insight into structural and orientational parameters . The component analysis of the potential dependent SERS spectra of cytochrome c552 provides the relative spectral contributions of the ferric and ferrous heme c . From Nernst plots, the potential of the redox transition and an apparent number of transferred electrons for the immobilized cyt c552 were obtained.…”

Section: Advantages In Usementioning

confidence: 99%

Spectroelectrochemical Sensing: Current Trends and Challenges

et al. 2019

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Spectroelectrochemistry (SEC) has been used for more than 50 years, but this set of techniques has not been widely used for quantitative analysis. For many years, no commercial instruments were available, which made very difficult to spread the use of SEC. Nowadays, only the creativity of the researchers is required to exploit the capabilities of SEC. This review is written with the aim of showing the potential of SEC, mainly for analytical chemistry. Here, we explain what SEC is, how analytical responses can be obtained, why these techniques are useful for sensors, with a brief description of its advantages in use, and, finally, we try to show the challenges that must be addressed in the next years. SEC can resolve interesting analytical problems using the high amount of data provided by this intrinsic trilinear technique. Given the quantitative analysis point of view of this review, the discussion of the SEC techniques is focused on UV/Vis absorption, photoluminescence and Raman SEC.

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“…Another vibrational spectroscopy technique for monitoring in situ bioelectrochemical systems is Raman spectroscopy, where surface enhanced resonance Raman spectroscopy is used to improve the signal (Silveira et al 2015, Ly et al 2011. Electronic spectra have also been used in the study of bioelectrochemical reactions, for example, the UV-vis spectroelectrochemical technique was used in the evaluation of ferredoxin from Schizosaccharomyces pombe (Wu et al 2011), where several electronic spectra at various applied potentials were obtained for this protein.…”

Section: In Situ Techniquesmentioning

confidence: 99%

Advances in enzyme bioelectrochemistry

Pereira

Sedenho

Souza

et al. 2018

An. Acad. Bras. Ciênc.

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Bioelectrochemistry can be defined as a branch of Chemical Science concerned with electron-proton transfer and transport involving biomolecules, as well as electrode reactions of redox enzymes. The bioelectrochemical reactions and system have direct impact in biotechnological development, in medical devices designing, in the behavior of DNA-protein complexes, in green-energy and bioenergy concepts, and make it possible an understanding of metabolism of all living organisms (e.g. humans) where biomolecules are integral to health and proper functioning. In the last years, many researchers have dedicated itself to study different redox enzymes by using electrochemistry, aiming to understand their mechanisms and to develop promising bioanodes and biocathodes for biofuel cells as well as to develop biosensors and implantable bioelectronics devices. Inside this scope, this review try to introduce and contemplate some relevant topics for enzyme bioelectrochemistry, such as the immobilization of the enzymes at electrode surfaces, the electron transfer, the bioelectrocatalysis, and new techniques conjugated with electrochemistry vising understand the kinetics and thermodynamics of redox proteins. Furthermore, examples of recent approaches in designing biosensors and biofuel developed are presented.

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SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes

Cited by 15 publications

References 46 publications

Advancing Techniques for Investigating the Enzyme–Electrode Interface

Advancing Techniques for Investigating the Enzyme–Electrode Interface

Spectroelectrochemical Sensing: Current Trends and Challenges

Advances in enzyme bioelectrochemistry

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