- Abstract:
-
Carbon monoxide dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2 . Several small molecules or ions are inhibitors and probes for different oxidation states of the unusual [Ni-4 Fe-4 S] cluster that forms the active site. The actions of these small probes on two enzymes-CODH ICh and CODH IICh -produced by Carboxydothermus hydrogenoformans have been studied by protein film voltammetry to compare their behaviour and to establish general characteristics. Whereas CODH I...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/cbic.201300270
-
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- Journal:
- Chembiochem : a European journal of chemical biology
- Volume:
- 14
- Issue:
- 14
- Pages:
- 1845-1851
- Publication date:
- 2013-09-05
- DOI:
- EISSN:
-
1439-7633
- ISSN:
-
1439-4227
- URN:
-
uuid:a5e1e74b-1940-4eb7-bf22-535f3f605fd3
- Source identifiers:
-
421069
- Local pid:
- pubs:421069
- Copyright date:
- 2013
Journal article
Investigations of two bidirectional carbon monoxide dehydrogenases from Carboxydothermus hydrogenoformans by protein film electrochemistry.
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