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M409884200v1
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Papers In Press, published online ahead of print November 10, 2004
J. Biol. Chem, 10.1074/jbc.M409884200
Submitted on August 27, 2004
Revised on November 2, 2004
Accepted on November 10, 2004

Spectroscopic and redox properties of a CooA homologue from carboxydothermus hydrogenoformans

Sayaka Inagaki, Chiaki Masuda, Tetsuhiro Akaishi, Hiroshi Nakajima, Shiro Yoshioka, Takehiro Ohta, Pal Biswajit, Teizo Kitagawa, and Shigetoshi Aono

Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi 444-8787

Corresponding Author: aono{at}ims.ac.jp

CooA is a CO-sensing transcriptional activator, which 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 His82 and the N-terminal -amino group were the axial ligands of the Fe(III) and Fe(II) hemes in Ch-CooA and that the N-terminal -amino group was replaced by CO upon CO binding. Two neutral ligands, His82 and the N-terminal -amino group, are coordinated to the Fe(III) heme in Ch-CooA while two negatively charged ligands, a thiolate from Cys75 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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