Carbon Monoxide Dehydrogenases.

  title={Carbon Monoxide Dehydrogenases.},
  author={Jae‐Hun Jeoung and Berta M. Martins and Holger Dobbek},
  journal={Methods in molecular biology},
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. 
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The aerobic CO dehydrogenase from Oligotropha carboxidovorans
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The discovery of a pathway of autotrophic growth is described in which carbon monoxide or carbon dioxide and hydrogen is used as the source of carbon and energy. Carbon monoxide dehydrogenase is the
Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide.
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OAK-B135 Metalloenzymes seem to ''come of age'' when their structures are known at atomic resolution, spectroscopic and catalytic properties are basically understood, and genetic expression systems
Carbon monoxide dehydrogenase reaction mechanism: a likely case of abnormal CO2 insertion to a Ni-H(-) bond.
A revised version of an earlier proposal for the catalytic cycle of Ni-containing CODH that agrees with available spectroscopic and structural data is put forward.
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The Ni-containing carbon monoxide dehydrogenase I from Carboxydothermus hydrogenoformans adsorbed on a pyrolytic graphite “edge” electrode catalyzes rapid CO2/CO interconversions at the thermodynamic
Orbital contributions to CO oxidation in Mo-Cu carbon monoxide dehydrogenase.
A molecular orbital analysis provides new insight into the mechanism of Mo/Cu carbon monoxide dehydrogenase, and reveals electronic structure contributions to reactivity that are remarkably similar
Structural basis of cyanide inhibition of Ni, Fe-containing carbon monoxide dehydrogenase.
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Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones.
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