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CODH‐IV: A High‐Efficiency CO‐Scavenging CO Dehydrogenase with Resistance to O2
CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2. Genomic analysis indicated that the metabolic functions of CODHs vary. The genome of Carboxydothermus hydrogenoformans encodes five CODHs (CODH‐I–V), of which CODH‐IV is found in a gene cluster near a peroxide‐reducing...
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Published in: | Angewandte Chemie International Edition 2017-11, Vol.56 (48), p.15466-15469 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2. Genomic analysis indicated that the metabolic functions of CODHs vary. The genome of Carboxydothermus hydrogenoformans encodes five CODHs (CODH‐I–V), of which CODH‐IV is found in a gene cluster near a peroxide‐reducing enzyme. Our kinetic and crystallographic experiments reveal that CODH‐IV differs from other CODHs in several characteristic properties: it has a very high affinity for CO, oxidizes CO at diffusion‐limited rate over a wide range of temperatures, and is more tolerant to oxygen than CODH‐II. Thus, our observations support the idea that CODH‐IV is a CO scavenger in defence against oxidative stress and highlight that CODHs are more diverse in terms of reactivity than expected.
Scavenger hunt: CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2. CODH‐IV is shown to differ from other CODHs. In particular, it acts as a CO scavenger in defence against oxidative stress, highlighting that CODHs are more diverse in terms of reactivity than expected. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201709261 |