[FeFe]-hydrogenase maturation: HydG-catalyzed synthesis of carbon monoxide.
J Am Chem Soc
; 132(27): 9247-9, 2010 Jul 14.
Article
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| MEDLINE
| ID: mdl-20565074
ABSTRACT
Biosynthesis of the unusual organometallic H-cluster at the active site of the [FeFe]-hydrogenase requires three accessory proteins, two of which are radical AdoMet enzymes (HydE, HydG) and one of which is a GTPase (HydF). We demonstrate here that HydG catalyzes the synthesis of CO using tyrosine as a substrate. CO production was detected by using deoxyhemoglobin as a reporter and monitoring the appearance of the characteristic visible spectroscopic features of carboxyhemoglobin. Assays utilizing (13)C-tyrosine were analyzed by FTIR to confirm the production of HbCO and to demonstrate that the CO product was synthesized from tyrosine. CO ligation is a common feature at the active sites of the [FeFe], [NiFe], and [Fe]-only hydrogenases; however, this is the first report of the enzymatic synthesis of CO in hydrogenase maturation.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Monóxido de Carbono
/
Hidrogenasas
Idioma:
En
Revista:
J Am Chem Soc
Año:
2010
Tipo del documento:
Article
País de afiliación:
Estados Unidos