A Tightly Bound Quinone Functions in the Ubiquinone Reaction Sites of Quinoprotein Alcohol Dehydrogenase of an Acetic Acid Bacterium,<i>Gluconobacter suboxydans</i>

Matsushita, Kazunobu; Kobayashi, Yoshiki; Mizuguchi, Mitsuhiro; Toyama, Hirohide; Adachi, Osao; Sakamoto, Kimitoshi; Miyoshi, Hideto

doi:10.1271/bbb.80363

Cited by 24 publications

(5 citation statements)

References 24 publications

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“…In addition, a subtle but exact electron density, into which a certain coordinate can be introduced, was found near heme 1 c in the cryo-EM maps of both ADH and AlDH (Figure S5). Based on their physiological roles, we concluded that UQ 10 was the most probable coordinate. , Reversed-phase high-performance liquid chromatography (HPLC) was performed for the organic extracts of the ADH and AlDH solutions, and the results also revealed the presence of UQ 10 (Figure S6). UQ 10 was quantified as only 0.04% of the molar amount of ADH and AlDH, indicating that UQ 10 was weakly and partly bound to the enzymes.…”

Section: Resultsmentioning

confidence: 99%

Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases

et al. 2023

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The efficient utilization of biomass fuels is a critical component of a sustainable energy economy. Via respiration, acetic acid bacteria can oxidize biomass ethanol into acetic acid using membrane-bound alcohol and aldehyde dehydrogenases (ADH and AlDH, respectively). Focusing on the ability of these enzymes to interact directly and electrically with electrode materials, we constructed a mediatorless bioanode for ethanol oxidation based on a direct electron transfer (DET)-type bienzymatic cascade by ADH and AlDH. The three-dimensional structural data of ADH and AlDH elucidated by cryo-electron microscopy were valuable for effectively designing electrode platforms with multi-walled carbon nanotubes (MWCNTs) and pyrene (Py) derivatives. DET-type bioelectrocatalysis by ADH and AlDH was improved by using 1-pyrene carboxylic acid-functionalized MWCNTs. The catalytic current densities for bienzymatic ethanol oxidation were recorded at the bioanodes modified by various ADH/AlDH ratios. The reaction model was constructed by focusing on the competitive adsorption of two enzymes on the electrode surface and the collection efficiency of the intermediately produced acetaldehyde. The power output of an ethanol/air biofuel cell using the bienzymatic bioanode reached 0.48 ± 0.01 mW cm–2, which is the highest value reported for ethanol biofuel cells. In addition, the Faraday efficiency of acetate production by the cell reached 100 ± 4%. This study will lead to efficient conversion of biomass fuels based on a multi-catalytic cascade system.

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Section: Resultsmentioning

confidence: 99%

Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases

et al. 2023

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“…Based on their physiological roles, we concluded that UQ10 was the most probable coordinate. 88,98 Reversed-phase high-performance liquid chromatography (HPLC) was performed for the organic extracts of the ADH and AlDH solutions, and the results also revealed the presence of UQ10 (Figure S6). UQ10 was quantified as only 0.04% of the molar amount of ADH and AlDH, indicating that UQ10 was weakly and partly bound to the enzymes.…”

Section: Membrane-bound Helixmentioning

confidence: 99%

Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases

Adachi

Miyata

Makino

et al. 2023

Preprint

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The efficient utilization of biomass fuels is a critical component of a sustainable energy economy. Via respiration, acetic acid bacteria can oxidize biomass ethanol into acetic acid using membrane-bound alcohol and aldehyde dehydrogenases (ADH and AlDH, respectively). Focusing on the ability of these enzymes to interact directly and electrically with electrode materials, we constructed a mediatorless bioanode for ethanol oxidation based on a direct electron transfer (DET)-type bienzymatic cascade by ADH and AlDH. The three-dimensional structural data of ADH and AlDH elucidated by cryo-electron microscopy were valuable for effectively designing electrode platforms with multi-walled carbon nanotubes (MWCNTs) and pyrene derivatives. DET-type bioelectrocatalysis by ADH and AlDH was improved by using 1-pyrene carboxylic acid-functionalized MWCNT. The catalytic current densities for bienzymatic ethanol oxidation were recorded at the bioanodes modified by various ADH/AlDH ratios. The reaction model was constructed by focusing on the competitive ad-sorption of two enzymes on the electrode surface and the collection efficiency of the intermediately produced acetaldehyde. The power output of an ethanol/air biofuel cell using the bienzymatic bioanode reached 0.48 ± 0.01 mW cm–2, which is the highest value reported for ethanol biofuel cells. In addition, the Faraday efficiency of acetate production by the cell reached 100 ± 4%. This study will lead to efficient conversion of biomass fuels based on a multi-catalytic cascade system.

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“…In addition, clear elongated densities were observed between heme 1 c and the membrane-bound region in the 3D maps of both rFDH-R and rFDH-O (Figure S8C and D). Based on the physiological role of FDH, we considered that UQ 10 was the most probable candidate for these densities. , Reverse-phase high-performance liquid chromatography (HPLC) was performed on the organic extracts of the rFDH solutions, and the results confirmed the presence of UQ 10 (Figure S9). UQ 10 was quantified as 1% of the molar amount of rFDH, indicating that UQ 10 bound weakly and partially to the enzymes.…”

Section: Resultsmentioning

confidence: 91%

Essential Insight of Direct Electron Transfer-Type Bioelectrocatalysis by Membrane-Bound d-Fructose Dehydrogenase with Structural Bioelectrochemistry

Suzuki,

Makino,

Miyata

et al. 2023

ACS Catal.

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Flavin adenine dinucleotide-dependent D-fructose dehydrogenase (FDH) from Gluconobacter japonicus NBRC3260, a membrane-bound heterotrimeric flavohemoprotein capable of direct electron transfer (DET)-type bioelectrocatalysis, was investigated from the perspective of structural biology, bioelectrochemistry, and protein engineering. DET-type reactions offer several benefits in biomimetics (e.g., biofuel cells, bioreactors, and biosensors) owing to their mediator-less configuration. FDH provides an intense DETtype catalytic signal; therefore, extensive research has been conducted on the fundamental principles and applications of biosensors. Structural analysis using cryo-electron microscopy and single-particle analysis has revealed the entire FDH structures with resolutions of 2.5 and 2.7 Å for the reduced and oxidized forms, respectively. The electron transfer (ET) pathway during the catalytic oxidation of D-fructose was investigated by using both thermodynamic and kinetic approaches. Structural analysis has shown the localization of the electrostatic surface charges around heme 2c in subunit II, and experiments using functionalized electrodes with a controlled surface charge support the notion that heme 2c is the electrode-active site. Furthermore, two aromatic amino acid residues (Trp427 and Phe489) were located in a possible long-range ET pathway between heme 2c and the electrode. Two variants (W427A and F489A) were obtained by site-directed mutagenesis, and their effects on DET-type activity were elucidated. The results have shown that Trp427 plays an essential role in accelerating long-range ET and triples the standard rate constant of heterogeneous ET according to bioelectrochemical analysis.

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A Tightly Bound Quinone Functions in the Ubiquinone Reaction Sites of Quinoprotein Alcohol Dehydrogenase of an Acetic Acid Bacterium,Gluconobacter suboxydans

Cited by 24 publications

References 24 publications

Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases

Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases

Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases

Essential Insight of Direct Electron Transfer-Type Bioelectrocatalysis by Membrane-Bound d-Fructose Dehydrogenase with Structural Bioelectrochemistry

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