Catalytic coupling of the active sites in acetyl-CoA synthase, a bifunctional CO-channeling enzyme.
Biochemistry
; 40(44): 13262-7, 2001 Nov 06.
Article
em En
| MEDLINE
| ID: mdl-11683635
ABSTRACT
Acetogenic bacteria contain acetyl-CoA synthase (ACS), an enzyme with two distinct nickel-iron-sulfur active sites connected by a tunnel through which CO migrates. One site reduces CO2 to CO, while the other synthesizes acetyl-CoA from CO, CoA, and the methyl group of another protein (CH3-CP). Rapid binding of CO2 and a two-electron reduction activates ACS. When CoA and CH3-CP bind ACS, CO is rerouted through the tunnel to the synthase site, and kinetic parameters at the reductase site are altered. Under these conditions, the rates of CO2 reduction and acetyl-CoA synthesis are synchronized by an ordered catalytic mechanism.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Acetato-CoA Ligase
/
Monóxido de Carbono
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2001
Tipo de documento:
Article