Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.

Bonam, Duane; Ludden, Paul W.

doi:10.1016/s0021-9258(18)61456-5

Cited by 138 publications

(72 citation statements)

References 40 publications

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“…The Coo hydrogenase cluster has been identified in 30 bacterial representatives, at particularly high frequency in Deltaproteobacteria (many sulfate reducers, e.g., Desulfovibrio vulgaris), Alpha-(e.g., Rhodospirillum rubrum) and Campylobacteria (Nautilia profundicola), Firmicutes (e.g., Carboxydothermus hydrogenoformans), Betaproteobacteria and Gammaproteobacteria (Schoelmerich and Müller, 2019). Phylogenetic analysis based on the large subunit CooH indicated that this hydrogenase was clustered together with those of R. rubrum, D. vulgaris and C. hydrogenoformans (Figure 6), which have been experimentally demonstrated to oxidize CO, producing carbon dioxide and hydrogen as products, through CooMKLXUHF complexes (Bonam and Ludden, 1987;Wu et al, 2005;Caffrey et al, 2007). Further, protein domain analyses by DELTA-BLAST and PSI-BLAST in NCBI showed that CooH contains three functional domains: two respiratory-chain NADH dehydrogenases and one nickel-dependent hydrogenase.…”

Section: Environmental Adaptations Of Sulfurimonas Revealed By Comparmentioning

confidence: 95%

Characterization of Sulfurimonas hydrogeniphila sp. nov., a Novel Bacterium Predominant in Deep-Sea Hydrothermal Vents and Comparative Genomic Analyses of the Genus Sulfurimonas

Wang

Jiang

et al. 2021

Front. Microbiol.

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Bacteria of the genus Sulfurimonas within the class Campylobacteria are predominant in global deep-sea hydrothermal environments and widespread in global oceans. However, only few bacteria of this group have been isolated, and their adaptations for these extreme environments remain poorly understood. Here, we report a novel mesophilic, hydrogen- and sulfur-oxidizing bacterium, strain NW10T, isolated from a deep-sea sulfide chimney of Northwest Indian Ocean.16S rRNA gene sequence analysis showed that strain NW10T was most closely related to the vent species Sulfurimonas paralvinellae GO25T with 95.8% similarity, but ANI and DDH values between two strains were only 19.20 and 24.70%, respectively, indicating that strain NW10 represents a novel species. Phenotypic characterization showed strain NW10T is an obligate chemolithoautotroph utilizing thiosulfate, sulfide, elemental sulfur, or molecular hydrogen as energy sources, and molecular oxygen, nitrate, or elemental sulfur as electron acceptors. Moreover, hydrogen supported a better growth than reduced sulfur compounds. During thiosulfate oxidation, the strain can produce extracellular sulfur of elemental α-S8 with an unknown mechanism. Polyphasic taxonomy results support that strain NW10T represents a novel species of the genus Sulfurimonas, and named as Sulfurimonas hydrogeniphila sp. nov. Genome analyses revealed its diverse energy metabolisms driving carbon fixation via rTCA cycling, including pathways of sulfur/hydrogen oxidation, coupled oxygen/sulfur respiration and denitrification. Comparative analysis of the 11 available genomes from Sulfurimonas species revealed that vent bacteria, compared to marine non-vent strains, possess unique genes encoding Type V Sqr, Group II, and Coo hydrogenase, and are selectively enriched in genes related to signal transduction and inorganic ion transporters. These phenotypic and genotypic features of vent Sulfurimonas may explain their thriving in hydrothermal environments and help to understand the ecological role of Sulfurimonas bacteria in hydrothermal ecosystems.

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Section: Environmental Adaptations Of Sulfurimonas Revealed By Comparmentioning

confidence: 95%

Characterization of Sulfurimonas hydrogeniphila sp. nov., a Novel Bacterium Predominant in Deep-Sea Hydrothermal Vents and Comparative Genomic Analyses of the Genus Sulfurimonas

Wang

Jiang

et al. 2021

Front. Microbiol.

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“…The amino acid sequences of CodhAB were also homologous to the CooFS proteins (41.7% and 50.3% identity, respectively) in Rhodospirillum rubrum . CooF mediates electron transfer from the CODH catalytic subunit CooS to hydrogenase and interacts directly with CooS 34 , 35 ; hence, spontaneous enzyme complex formation of CodhA and CodhB is easily predictable. Accordingly, Fdh3C-CodhA and Fdh3B-CodhA were designed and constructed.…”

Section: Resultsmentioning

confidence: 99%

Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

et al. 2022

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Ferredoxin-dependent metabolic engineering of electron transfer circuits has been developed to enhance redox efficiency in the field of synthetic biology, e.g., for hydrogen production and for reduction of flavoproteins or NAD(P)+. Here, we present the bioconversion of carbon monoxide (CO) gas to formate via a synthetic CO:formate oxidoreductase (CFOR), designed as an enzyme complex for direct electron transfer between non-interacting CO dehydrogenase and formate dehydrogenase using an electron-transferring Fe-S fusion protein. The CFOR-introduced Thermococcus onnurineus mutant strains showed CO-dependent formate production in vivo and in vitro. The maximum formate production rate from purified CFOR complex and specific formate productivity from the bioreactor were 2.2 ± 0.2 μmol/mg/min and 73.1 ± 29.0 mmol/g-cells/h, respectively. The CO-dependent CO2 reduction/formate production activity of synthetic CFOR was confirmed, indicating that direct electron transfer between two unrelated dehydrogenases was feasible via mediation of the FeS-FeS fusion protein.

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“…However, in term of performances for potential future applications, the catalytic efficiencies of these thermophilic enzymes are limited under ambient conditions. On the other hand, CODH from the mesophile bacterium R. rubrum has been largely characterized since the late 80s, 20,21,22,23 although studies have been limited in the last decade. R. rubrum possesses a single monofunctional CODH (homologue to ChCODH-I), involved in the water gas shift reaction (CO + H2O  CO2 + H2), enabling the bacterium to use CO as sole energy source.…”

Section: Efficient Electrochemical Co 2 /Co Interconversion By An Engineered Carbon Monoxide Dehydrogenase On a Gas-diffusion Carbon Nanomentioning

confidence: 99%

Efficient Electrochemical CO₂/CO Interconversion by an Engineered Carbon Monoxide Dehydrogenase on a Gas-Diffusion Carbon Nanotube-Based Bioelectrode

et al. 2021

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Carbon monoxide dehydrogenase reversibly catalyzes the oxidation of CO into CO2. The monofunctional enzyme from Rhodospirillum rubrum (RrCODH) has been extensively characterized in the past, although its use and investigation by bioelectrochemistry have been limited. Here, we developed a heterologous system yielding a highly stable and active recombinant RrCODH in one-step purification, with a CO oxidation activity reaching a maximum of 26,500 U mg -1 , making RrCODH the most active CODH under ambient conditions described so far. Electron Paramagnetic Resonance was used to precisely characterize the recombinant RrCODH, demonstrating the integrity of the active site. Selective CO2/CO interconversion with maximum turnover frequencies of 150 s -1 for CO oxidation (1.5 mA cm -2 at 250 mV overpotential) and 420 s -1 for CO2 reduction (4.2 mA cm -2 at 180 mV overpotential) are catalyzed by the recombinant RrCODH immobilized on MWCNT electrodes modified with 1-pyrenebutyric acid adamantyl amide (MWCNT ADA ), either in classic three-electrode cell or in specifically-designed CO2/CO-diffusing electrodes. This functional device is stable for hours, and for at least 800,000 turnover numbers. The performances of recombinant RrCODH-modified MWCNT ADA are closed to the best metal-based and molecular-based catalysts. These results greatly increase the benchmark for bioelectrocatalysis of reversible CO2 conversion.

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Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.

Cited by 138 publications

References 40 publications

Characterization of Sulfurimonas hydrogeniphila sp. nov., a Novel Bacterium Predominant in Deep-Sea Hydrothermal Vents and Comparative Genomic Analyses of the Genus Sulfurimonas

Characterization of Sulfurimonas hydrogeniphila sp. nov., a Novel Bacterium Predominant in Deep-Sea Hydrothermal Vents and Comparative Genomic Analyses of the Genus Sulfurimonas

Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

Efficient Electrochemical CO₂/CO Interconversion by an Engineered Carbon Monoxide Dehydrogenase on a Gas-Diffusion Carbon Nanotube-Based Bioelectrode

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Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.

Cited by 138 publications

References 40 publications

Characterization of Sulfurimonas hydrogeniphila sp. nov., a Novel Bacterium Predominant in Deep-Sea Hydrothermal Vents and Comparative Genomic Analyses of the Genus Sulfurimonas

Characterization of Sulfurimonas hydrogeniphila sp. nov., a Novel Bacterium Predominant in Deep-Sea Hydrothermal Vents and Comparative Genomic Analyses of the Genus Sulfurimonas

Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

Efficient Electrochemical CO2/CO Interconversion by an Engineered Carbon Monoxide Dehydrogenase on a Gas-Diffusion Carbon Nanotube-Based Bioelectrode

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Efficient Electrochemical CO₂/CO Interconversion by an Engineered Carbon Monoxide Dehydrogenase on a Gas-Diffusion Carbon Nanotube-Based Bioelectrode