Protonation and inhibition of Nitrosomonas europaea cytochrome c peroxidase observed with protein film voltammetry

Elliott, Sean J.; Bradley, Amy L.; Arciero, David M.; Hooper, Alan B.

doi:10.1016/j.jinorgbio.2006.09.009

Cited by 11 publications

(10 citation statements)

References 24 publications

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“…Electrochemical studies on C c P confirm a role for PCET at the heme sites with appearance of pH-dependent electrochemistry over the range pH = 5–11 (Figure ). , Protein film voltammetry (PFV) was used to investigate the pH dependence of C c P (Figures and ). The data in Figure were fit to a two p K a model in which the oxidized and reduced states can be protonated independently.…”

Section: Pcet In Biology and Model Systemsmentioning

confidence: 91%

Proton-Coupled Electron Transfer

et al. 2012

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An initial review (PCET1) on proton-coupled electron transfer (PCET) by Huynh and Meyer appeared in Chemical Reviews in 2007. 1 This is a perennial review, a follow up on the original. It was intended for the special Chemical Reviews edition on Proton Coupled Electron Transfer that appeared in December, 2010 (Volume 110, Issue 12 Pages 6937-710). The reader is referred to it with articles on electrochemical approaches to studying PCET by Costentin and coworkers, 2 theory of electron proton transfer reactions by Hammes-Schiffer and coworkers, 3 proton-coupled electron flow in proteins and enzymes by Gray and coworkers, 4 and the thermochemistry of proton-coupled electron transfer by Mayer and coworkers. 5 Coverage for the current review is intended to be broad, covering all aspects of the topic comprehensively with literature coverage overlapping with the later references in PCET1 until late 2010. There is a growing understanding of the importance of PCET in chemistry and biology and its implications for catalysis and energy conversion. This has led to a series of informative reviews that have appeared since 2007. They include: "The possible role of Proton-coupled electron Transfer (PCET) in Water oxidation by Photosystem II" by Meyer and coworkers in 2007, 6 "Theoretical studies of proton-coupled electron transfer: Models and concepts relevant to bioenergetics" by Hammes-Schiffer and coworkers in 2008, 7 "Electrochemical Approach to the Mechanistic Study of Proton-Coupled Electron Transfer" by Costentin in 2008, 8 "Proton-Coupled Electron Transfer in Biology: Results from Synergistic Studies in Natural and Model Systems" by Nocera and Reece in 2009, 9 and "Integrating Proton-Coupled Electron Transfer and Excited States" by Meyer and coworkers in 2010. 10

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Section: Pcet In Biology and Model Systemsmentioning

confidence: 91%

Proton-Coupled Electron Transfer

et al. 2012

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“…In parallel to our previous work conducted with the Pseudomonas and Nitrosomonas , C c P enzymes, we have used PFV at graphite electrodes to observe the redox chemistry of wild-type Gs CcpA. The addition of substrate results in electrocatalytic limiting currents that are related to the kinetics of the enzyme, and analysis of the data shows that catalytic electrochemistry is low in reduction potential, is fast and reversible in a cyclic voltammetry experiment (i.e., no hysteresis), possesses a shape of the electrocatalytic wave that indicates a one-electron redox process, and yields limiting currents that when treated as enzymatic velocities predict K m values for substrate and maximal activities as a function of pH that agree with solution measurements.…”

Section: Discussionmentioning

confidence: 99%

“…The Gs CcpA gene product has recently been shown to be a highly basic cytochrome c peroxidase that is quite similar to the canonical diheme peroxidases, including the disposition of the two heme cofactors, the observation of a Ca 2+ ion bound at the interface of the two heme-bearing domains common to all bacterial C c P enzymes, − and the requirement for prereduction of the His/Met-ligated high-potential heme ( H -heme) to attain activity at the peroxidatic active site ( L -heme) . As indicated in Table , the majority of bacterial heme peroxidases require reductive activation, ,,,, aside from a small number of C c P enzymes, including that from Nitrosomonas europaea ( Ne ). ,,− The overall process of reductive activation begins with the low-midpoint potential − L -heme existing in the oxidized state, with a bis-His-ligated coordination environment. Reduction of the high-potential heme ( H -heme) by one electron causes a conformational change in the L-loop region containing the distal His ligand, as well as two other loop regions (Figure A, in which loops are labeled 1–3).…”

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confidence: 99%

Geobacter sulfurreducens Cytochrome c Peroxidases: Electrochemical Classification of Catalytic Mechanisms

et al. 2011

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Bacterial cytochrome c peroxidase (CcP) enzymes are diheme redox proteins that reduce hydrogen peroxide to water. They are canonically characterized by a peroxidatic (called L, for “low reduction potential”) active site heme, and a secondary heme (H, for “high reduction potential”) associated with electron transfer, and an enzymatic activity that exists only when the H-heme is pre-reduced to the FeII oxidation state. The pre-reduction step results in a conformational change at the active site itself, where a histidine-bearing loop will adopt an “open” conformation allowing hydrogen peroxide to bind to the FeIII of the L-heme. Notably, the enzyme from Nitrosomonas europaea does not require pre-reduction. Previously, we have shown that protein film voltammetry (PFV) is a highly useful tool in distinguishing the electrocatalytic mechanisms of the Nitromonas-type of enzyme from other CcPs. Here, we apply PFV to the recently described enzyme from Geobacter sulfurreducens, and the Geobacter S134P/V135K double mutant, which has been shown to be similar to the canonical sub-class of peroxidases and the Nitrosomonas sub-class of enzymes, respectively. Here we find that the wild-type Geobacter CcP is indeed similar electrochemically to the bacterial CcPs that require reductive activation, yet the S134P/V135K mutant shows two phases of electrocatalysis: one that is low in potential, like the wild-type enzyme, and a second, higher-potential phase that has a potential dependent upon substrate binding and pH, yet is at a potential that is very similar to the H-heme. These findings are interpreted in terms of a model where rate-limiting intra-protein electron transfer governs the catalytic performance of the S134P/V135K enzyme.

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“…In addition, the binding properties of inhibitors to the reduced and oxidized active sites were characterized (Figure 22). 750 Besides hydrogenase and formate dehydrogenase, the catalytic mechanisms of nitrate reductases, 751 acetyl-CoA synthase, 752 and cytochrome c peroxidase 753 have also been investigated by using protein film voltammetry. As the protein film voltammetry is an extensive research area, many review articles have provided a detailed and comprehensive summary of the principle, characteristics, and applications of this technology.…”

Section: Investigation Of Oxidoreductase Catalytic Mechanisms Via Bio...mentioning

confidence: 99%

Fundamentals, Applications, and Future Directions of Bioelectrocatalysis

et al. 2020

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Bioelectrocatalysis is an interdisciplinary research field combining biocatalysis and electrocatalysis via the utilization of materials derived from biological systems as catalysts to catalyze the redox reactions occurring at an electrode. Bioelectrocatalysis synergistically couples the merits of both biocatalysis and electrocatalysis. The advantages of biocatalysis include high activity, high selectivity, wide substrate scope, and mild reaction conditions. The advantages of electrocatalysis include the possible utilization of renewable electricity as an electron source and high energy conversion efficiency. These properties are integrated to achieve selective biosensing, efficient energy conversion, and the production of diverse products. This review seeks to systematically and comprehensively detail the fundamentals, analyze the existing problems, summarize the development status and applications, and look toward the future development directions of bioelectrocatalysis. First, the structure, function, and modification of bioelectrocatalysts are discussed. Second, the essentials of bioelectrocatalytic systems, including electron transfer mechanisms, electrode materials, and reaction medium, are described. Third, the application of bioelectrocatalysis in the fields of biosensors, fuel cells, solar cells, catalytic mechanism studies, and bioelectrosyntheses of high-value chemicals are systematically summarized. Finally, future developments and a perspective on bioelectrocatalysis are suggested.

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Protonation and inhibition of Nitrosomonas europaea cytochrome c peroxidase observed with protein film voltammetry

Cited by 11 publications

References 24 publications

Proton-Coupled Electron Transfer

Proton-Coupled Electron Transfer

Geobacter sulfurreducens Cytochrome c Peroxidases: Electrochemical Classification of Catalytic Mechanisms

Fundamentals, Applications, and Future Directions of Bioelectrocatalysis

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