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Carbon is the basis of all organic matter on Earth, and is recycled through the ecosystem in two primary processes: one in which carbon is exchanged among living organisms, and one in which carbon is cycled over long periods of time through fossilized organic remains, weathering of rocks, and volcanic activity. Human activities, including increased agricultural practices and the burning of fossil fuels, has greatly affected the balance of the natural carbon cycle.
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Atmospheric CO2 penetrates the concrete's pores and, in the presence of moisture, forms carbonic acid, which then reacts with calcium hydroxide in the hydrated cement, forming calcium carbonate. This process reduces the concrete's volume and is termed carbonation shrinkage.
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Carbon Monoxide Dehydrogenases.

Jae-Hun Jeoung1, Berta M Martins1, Holger Dobbek2

  • 1Institute of Biology, Structural Biology and Biochemistry, Humboldt-Universität zu Berlin, Berlin, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|October 15, 2018
PubMed
Summary
This summary is machine-generated.

Carbon monoxide dehydrogenases (CODHs) reversibly oxidize CO to CO2. This overview covers two distinct classes of CODHs, highlighting their different structures and metal active sites.

Keywords:
CO2Carbon monoxide dehydrogenaseIron–sulfur clustersNi enzymescluster C

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Carbon monoxide dehydrogenases (CODHs) are crucial enzymes catalyzing the reversible conversion of carbon monoxide (CO) to carbon dioxide (CO2).
  • This reaction involves the transfer of two electrons and two protons, playing a key role in carbon cycling and energy metabolism.
  • Two distinct classes of CODHs have been identified, differing in their evolutionary origins and active site compositions.

Purpose of the Study:

  • To provide a comprehensive overview of the fundamental properties of carbon monoxide dehydrogenases (CODHs).
  • To differentiate between the two known classes of CODHs based on their structural scaffolds and active site transition metals.
  • To elucidate the catalytic mechanism and biological significance of these enzymes.

Main Methods:

  • Literature review and synthesis of existing research on CODHs.
  • Comparative analysis of the structural and biochemical characteristics of the two CODH classes.
  • Description of the catalytic mechanisms and electron transfer pathways.

Main Results:

  • Detailed description of the two distinct classes of CODHs, emphasizing their independent evolutionary pathways.
  • Characterization of the unique transition metal-based active sites present in each class.
  • Explanation of the reversible CO oxidation reaction catalyzed by both enzyme types.

Conclusions:

  • The existence of two separate CODH classes highlights convergent evolution in enzyme active site design.
  • Understanding these enzymes is vital for fields ranging from industrial catalysis to microbial ecology.
  • Further research into CODHs can unlock new biotechnological applications and insights into early life evolution.