Control of carbon monoxide dehydrogenase orientation by site-specific immobilization enables direct electrical contact between enzyme cofactor and solid surface [PDF]
Communications Biology, 2022 Control over the orientation of carbon monoxide dehydrogenase on electrode surfaces is demonstrated and designed for other redox enzymes to promote direct electron transfer in bioelectrocatalytic systems.
Stacy Simai Reginald +7 more
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Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase. [PDF]
J Inorg Biochem, 2022 Carbon monoxide dehydrogenase (CODH) plays an important role in the processing of one‐carbon gases carbon monoxide and carbon dioxide. In CODH enzymes, these gases are channeled to and from the Ni‐Fe‐S active sites using hydrophobic cavities. In this work, we investigate these gas channels in a monofunctional CODH from
Biester A, Dementin S, Drennan CL.
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Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase [PDF]
eLife, 2018 The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway.
Elizabeth C Wittenborn +8 more
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Evidence for horizontal gene transfer of anaerobic carbon monoxide dehydrogenases [PDF]
Frontiers in Microbiology, 2012 Carbon monoxide (CO) is commonly known as a toxic gas, yet it is used by both aerobic and anaerobic bacteria and many archaea. In this study, we determined the prevalence of anaerobic carbon monoxide dehydrogenases (anaerobic CODHs, or [Ni,Fe]-CODHs) in ...
Stephen eTechtmann +4 more
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“Candidatus Galacturonibacter soehngenii” Shows Acetogenic Catabolism of Galacturonic Acid but Lacks a Canonical Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Complex [PDF]
Frontiers in Microbiology, 2020 Acetogens have the ability to fixate carbon during fermentation by employing the Wood-Ljungdahl pathway (WLP), which is highly conserved across Bacteria and Archaea.
Laura C. Valk +7 more
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Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase. [PDF]
J Biol Chem, 2019 The nickel-dependent carbon monoxide dehydrogenase (CODH) employs a unique heterometallic nickel-iron-sulfur cluster, termed the C-cluster, to catalyze the interconversion of CO and CO2 Like other complex metalloenzymes, CODH requires dedicated assembly machinery to form the fully intact and functional C-cluster.
Wittenborn EC +6 more
europepmc +5 more sources
Anaerobic carbon monoxide dehydrogenase diversity in the homoacetogenic hindgut microbial communities of lower termites and the wood roach. [PDF]
PLoS ONE, 2011 Anaerobic carbon monoxide dehydrogenase (CODH) is a key enzyme in the Wood-Ljungdahl (acetyl-CoA) pathway for acetogenesis performed by homoacetogenic bacteria.
Eric G Matson +2 more
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Nickel model complexes to mimic carbon monoxide dehydrogenase reactions. [PDF]
Chem SciNickel model complexes inspired by CODH active sites offer crucial insights into CO2/CO interconversion mechanisms, guiding the development of efficient and selective synthetic catalysts for CO2 conversion.
Yoo C, Choi J, Lee Y.
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Heterologous Production of an Energy-Conserving Carbon Monoxide Dehydrogenase Complex in the Hyperthermophile Pyrococcus furiosus [PDF]
Frontiers in Microbiology, 2016 Carbon monoxide (CO) is an important intermediate in anaerobic carbon fixation pathways in acetogenesis and methanogenesis. In addition, some anaerobes can utilize CO as an energy source.
Gerrit Jan Schut +4 more
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Clinical characterization of 39 patients with autoimmune pulmonary alveolar proteinosis [PDF]
Journal of International Medical ResearchObjectives We aimed to explore the clinical manifestations, examination findings, diagnostic methods, and treatment efficacy of patients with pulmonary alveolar proteinosis and improve clinicians' understanding of this disease. Methods We retrospectively
Yan-Fen Zhong, Xiao Lv
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