Results 171 to 180 of about 23,949 (213)

Optimizing hyperbaric oxygen initiation time in carbon monoxide poisoning: a 3-hour window enhances neurological recovery via lactate clearance. [PDF]

Open Med (Wars)
Xu D, Xu X, Sun H, Xu J, Fei D, Shen Y.
europepmc   +1 more source

Investigating the native functions of [NiFe]-CODH through genomic context analysis. [PDF]

Elife
Böhm M, Land H.
europepmc   +1 more source

Distribution of carbon monoxide-oxidizing microorganisms along a chronosequence on Piton De La Fournaise volcano

Wildbur C, Dawson RA, Roy S, Ah-Peng C, Espenberg M, Hernández M.   +5 more
europepmc   +1 more source

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Construction of multiple metagenome assembled genomes containing carbon monoxide dehydrogenases from anaerobic carbon monoxide enrichment cultures

Archives of Microbiology, 2023
Despite its toxicity to many organisms, including most prokaryotes, carbon monoxide (CO) is utilized by some aerobic and anaerobic prokaryotes. Hydrogenogenic CO utilizers employ carbon monoxide dehydrogenase (CODH) and energy-converting hydrogenase (ECH) to oxidize CO and reduce protons to produce H2.
Nishida, Shiho, Omae, Kimiho, Inoue, Masao, Sako, Yoshihiko, Kamikawa, Ryoma, Yoshida, Takashi   +5 more
openaire   +2 more sources

Carbon-monoxide dehydrogenase

1993
Carbon monoxide (CO) is metabolized by a wide range of microorganisms according to the following reversible reaction: (5-1) Various aerobic bacteria including species of Pseudomonas, Alcaligenes, Bacillus, Arthrobacter, Azotobacter, and Azotomonas are capable of CO oxidation by using a molybdopterin-iron-sulfur-flavin-containing enzyme ...
Dietmar Schomburg, Margit Salzmann, Dörte Stephan   +2 more
openaire   +2 more sources

Carbon Monoxide Dehydrogenases

2018
Carbon monoxide dehydrogenases (CODHs) catalyze the reversible oxidation of CO with water to CO2, two electrons, and two protons. Two classes of CODHs exist, having evolved from different scaffolds featuring active sites built from different transition metals. The basic properties of both classes are described in this overview chapter.
Jae-Hun, Jeoung, Berta M, Martins, Holger, Dobbek   +2 more
openaire   +2 more sources

Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate

JBIC Journal of Biological Inorganic Chemistry, 2002
Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum reversibly catalyzes the oxidation of CO to CO(2) at the active site C-cluster. In this article, the reduction of CO(2) to formate is reported as a slow side reaction catalyzed by both Ni-containing CODH and Ni-deficient CODH. Recently, the structures of R.
Jongyun, Heo, Lars, Skjeldal, Christopher R, Staples, P W, Ludden   +3 more
openaire   +2 more sources

Redox titrations of carbon monoxide dehydrogenase from Clostridium thermoaceticum

Biochemistry, 1992
Redox titrations of carbon monoxide dehydrogenase (CODH) from Clostridium thermoaceticum were performed using the reductant CO and the oxidant thionin. Titrations were followed at 420 nm, a wavelength sensitive to redox changes of the iron-sulfur clusters in the enzyme. When CODH was oxidized by just enough thionin to maximize A420, two molecules of CO
W, Shin, P R, Stafford, P A, Lindahl
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X-Ray Crystallography of Carbon Monoxide Dehydrogenases

2018
Carbon monoxide dehydrogenases (CODHs) are central players in the biogeochemical carbon monoxide (CO) cycle and have been extensively studied from the ecological level to the structural/molecular level. Of the two types of CODHs, the oxygen-tolerant CODHs use a bimetallic [CuSMo(=O)OH] center connected to the protein via a pyranopterin cofactor ...
Jae-Hun, Jeoung, Berta M, Martins, Holger, Dobbek   +2 more
openaire   +2 more sources