Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas

Cordas, Cristina M.; Moura, Isabel; Moura, José J. G.

doi:10.1016/j.bioelechem.2008.04.019

Cited by 15 publications

(11 citation statements)

References 34 publications

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“…S1). Also, electrochemically‐activated Hase exhibits an H + reduction signal starting at −0.60 V (Figure , inset), in agreement with the reported behavior of a potential‐driven activated enzyme, which is slightly different from the chemically activated Hase, probably because the starting state is different when using the two activation methodologies, as previously reported . H 2 production was confirmed through GC analysis (see supporting information, Fig.…”

Section: Resultssupporting

confidence: 90%

“…Several processes can be observed, indexed as I, II and III, matching the various metallic redox center responses described in the literature, namely the distal [4Fe‐4S] cluster, the Ni(III)/Ni(II) active center transition, and the [3Fe‐4S] cluster, although cathodic peak III c appears slightly shifted towards more positive potentials. Redox center responses indicate a partially‐active Hase within the films, as observed in different conditions for this type of hydrogenases . The enzyme had been activated by either overnight incubation with H 2 , or by multiple potential cycling at low scan rate.…”

Section: Resultsmentioning

confidence: 80%

“…The enzyme contains one additional [3Fe‐4S] and two [4Fe‐4S] centers involved in transporting electrons to and from the active site, buried within the protein core (30 Å from the surface) . Hase presents different redox states associated to its active (fully reduced) and inactive (oxidized) states; the enzyme's direct electron transfer properties, and the possibility of electrochemically controlling its redox state (and consequently its activation or inactivation) were already demonstrated …”

Section: Introductionmentioning

confidence: 99%

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Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

et al. 2016

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In the present work, Ion Jelly films based on 1‐ethyl‐3‐methylimidazolium ethylsulfate, with incorporated redox proteins and enzymes were deposited on carbon screen‐printed electrodes (SPEs), and their electrochemical characterization was attained. Ion Jelly synthesis was carried out simultaneously with protein incorporation in its structure, followed by a maturation step under controlled atmosphere (4 days at 4 °C and water activity (aw) of 0.76). The electrochemical response of the material was characterized, and a sandwich‐type fuel cell configuration was subsequently built, consisting of two SPEs containing two independent Ion Jelly discs in the middle; one disc incorporated Desulfovibrio gigas cytochrome c3 and [NiFe]‐hydrogenase, while the other disc contained aldehyde oxidoreductase, constituting the biocathode and bioanode of the cell, respectively. Cell voltage increased with time in the presence of benzaldehyde, in agreement with a successful electronic pathway across the cell and the concomitant aldehyde oxidoreductase enzymatic activity. In the cathodic side assays, hydrogenase showed catalytic activity towards H+ reduction to H2.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 80%

Section: Introductionmentioning

confidence: 99%

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Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

et al. 2016

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“…One can anticipate that this is much more difficult, given the lower redox potentials of these. The proximal and distal clusters are considerably more reducing than the medial cluster, with reduction potentials of − 290 to − 360 mV [7,[9][10][11][12][13]. Following the reduction of the medial cluster, we therefore analyzed the EPR spectra for signs of reduction of also the proximal and distal clusters.…”

Section: +mentioning

confidence: 99%

“…The reduction potentials of the proximal and distal [4Fe-4S] clusters have been determined to −290 to −360 mV [7,[9][10][11][12][13]. The medial [3Fe-4S] cluster on the other hand, is more oxidizing with a potential of −70-+100 mV in known cases.…”

Section: Introductionmentioning

confidence: 99%

Photoinduced reduction of the medial FeS center in the hydrogenase small subunit HupS from Nostoc punctiforme

Raleiras

Hammarström

Lindblad

et al. 2015

Journal of Inorganic Biochemistry

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Linking Bacterial Metabolism to Graphite Cathodes: Electrochemical Insights into the H₂‐Producing Capability of Desulfovibrio sp.

et al. 2012

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Microbial biocathodes allow converting and storing electricity produced from renewable sources in chemical fuels (e.g., H(2) ) and are, therefore, attracting considerable attention as alternative catalysts to more expensive and less available noble metals (notably Pt). Microbial biocathodes for H(2) production rely on the ability of hydrogenase-possessing microorganisms to catalyze proton reduction, with a solid electrode serving as direct electron donor. This study provides new chemical and electrochemical data on the bioelectrocatalytic activity of Desulfovibrio species. A combination of chronoamperometry, cyclic voltammetry, and impedance spectroscopy tests were used to assess the performance of the H(2) -producing microbial biocathode and to shed light on the involved electron transfer mechanisms. Cells attached onto a graphite electrode were found to catalyze H(2) production for cathode potentials more reducing than -900 mV vs. standard hydrogen electrode. The highest obtained H(2) production was 8 mmol L(-1) per day, with a Coulombic efficiency close to 100 %. The electrochemical performance of the biocathode changed over time probably due to the occurrence of enzyme activation processes induced by extended electrode polarization. Remarkably, H(2) (at least up to 20 % v/v) was not found to significantly inhibit its own production.

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Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas

Cited by 15 publications

References 34 publications

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

Photoinduced reduction of the medial FeS center in the hydrogenase small subunit HupS from Nostoc punctiforme

Linking Bacterial Metabolism to Graphite Cathodes: Electrochemical Insights into the H₂‐Producing Capability of Desulfovibrio sp.

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Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas

Cited by 15 publications

References 34 publications

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

Photoinduced reduction of the medial FeS center in the hydrogenase small subunit HupS from Nostoc punctiforme

Linking Bacterial Metabolism to Graphite Cathodes: Electrochemical Insights into the H2‐Producing Capability of Desulfovibrio sp.

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Linking Bacterial Metabolism to Graphite Cathodes: Electrochemical Insights into the H₂‐Producing Capability of Desulfovibrio sp.