Spectroscopic and redox properties of a CooA homologue from Carboxydothermus hydrogenoformans.
J Biol Chem
; 280(5): 3269-74, 2005 Feb 04.
Article
en En
| MEDLINE
| ID: mdl-15537640
CooA is a CO-sensing transcriptional activator that contains a b-type heme as the active site for sensing its physiological effector, CO. In this study, the spectroscopic and redox properties of a new CooA homologue from Carboxydothermus hydrogenoformans (Ch-CooA) were studied. Spectroscopic and mutagenesis studies revealed that His-82 and the N-terminal alpha-amino group were the axial ligands of the Fe(III) and Fe(II) hemes in Ch-CooA and that the N-terminal alpha-amino group was replaced by CO upon CO binding. Two neutral ligands, His-82 and the N-terminal alpha-amino group, are coordinated to the Fe(III) heme in Ch-CooA, whereas two negatively charged ligands, a thiolate from Cys-75 and the nitrogen atom of the N-terminal Pro, are the axial ligands of the Fe(III) heme in Rr-CooA. The difference in the coordination structure of the Fe(III) heme resulted in a large positive shift of redox potentials of Ch-CooA compared with Rr-CooA. Comparing the properties of Ch-CooA and Rr-CooA demonstrates that the essential elements for CooA function will be: (i) the heme is six-coordinate in the Fe(III), Fe(II), and Fe(II)-CO forms; (ii) the N-terminal is coordinated to the heme as an axial ligand, and (iii) CO replaces the N-terminal bound to the heme upon CO binding.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacterias Anaerobias
/
Proteínas Bacterianas
/
Hemoproteínas
Idioma:
En
Revista:
J Biol Chem
Año:
2005
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos