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Papers In Press, published online ahead of print June 21, 2002
J. Biol. Chem, 10.1074/jbc.M204559200
Submitted on May 9, 2002
Revised on June 17, 2002
Accepted on June 21, 2002
Center for Integrative Bioscience, Okazaki National Research Institutes, Okazaki 444-8585
Corresponding Author: teizo{at}ims.ac.jp
The heme environments of Met95 and His77 mutants of the isolated heme-bound PAS domain (Ec DOS PAS) of a direct oxygen sensing protein from E. coli (Ec Dos) were investigated with resonance Raman (RR) spectroscopy and compared to the wild type (WT) enzyme. The RR spectra of both the reduced and oxidized WT enzyme were characteristic six-coordinated low-spin complexes from pH 4 to 10. The time-resolved RR spectra of the photo-dissociated CO-WT complex had an Fe-His stretching band at 214 cm-1, and the Fe-CO stretching vs C-O stretching plot of CO-WT Ec DOS PAS fell on the line of His-coordinated heme proteins. The photo-dissociated CO-His77Ala mutant complex did not yield the Fe-His stretching band but gave a Fe-imidazole stretching band in the presence of imidazole. The RR spectrum of the oxidized Met95Ala mutant was that of a six-coordinated low-spin complex, i.e. the same as that of the WT enzyme, whereas the reduced mutant appeared to contain a five-coordinated heme complex. Taken together, we suggest that the heme of the reduced WT enzyme is coordinated by His77 and Met95, and that Met95 is displaced by CO and O2. Presumably, the protein conformational change that occurs on exchange of an unknown ligand for Met95 following heme reduction, may lead to activation of the phosphodiesterase domain of Ec Dos.
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