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J. Biol. Chem., Vol. 277, Issue 36, 32650-32658, September 6, 2002
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From the The heme environments of Met95
and His77 mutants of the isolated heme-bound PAS domain
(Escherichia coli DOS PAS) of a direct oxygen sensing
protein from E. coli (E. coli DOS) were
investigated with resonance Raman (RR) spectroscopy and compared with
the wild type (WT) enzyme. The RR spectra of both the reduced and
oxidized WT enzyme were characteristic of six-coordinate low
spin heme complexes from pH 4 to 10. The time-resolved RR spectra of
the photodissociated CO-WT complex had an iron-His stretching band (
Stationary and Time-resolved Resonance Raman Spectra of
His77 and Met95 Mutants of the Isolated Heme
Domain of a Direct Oxygen Sensor from Escherichia coli*
,
**
School of Advanced Sciences, The Graduate
University for Advanced Studies, Shonan Village, Hayama, Kanagawa
240-0193, Japan, § Institute of Multidisciplinary Research
for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku,
Sendai 980-8577, Japan, ¶ Molecular Photoscience Research Center,
Kobe University, 1-1 Rokkodai, Nada-ku, Kobe 657-8501, Japan, and
Center for Integrative Bioscience, Okazaki National Research
Institutes, Myodaiji, Okazaki, Aichi 444-8585, Japan
Fe-His) at 214 cm
1, and the
Fe-CO versus CO plot of
CO-WT E. coli DOS PAS fell on the line of
His-coordinated heme proteins. The photodissociated CO-H77A
mutant complex did not yield the Fe-His band but gave a
Fe-Im band in the presence of imidazole. The RR spectrum
of the oxidized M95A mutant was that of a six-coordinate low
spin complex (i.e. the same as that of the WT enzyme),
whereas the reduced mutant appeared to contain a five-coordinate
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 upon exchange
of an unknown ligand for Met95 following heme reduction may
lead to activation of the phosphodiesterase domain of E. coli DOS.
*
This study was supported by a Grant-in-Aid for Scientific
Research 14001004 from the Ministry of Education, Culture, Sports, Science, and Technology, Japan (to T. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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