Structure and Function of the Heme-based Gas-sensing Proteins.
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Accession number;02A0304365
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| Title;Structure and Function of the Heme-based Gas-sensing Proteins. |
| Author;
AONO SHIGETOSHI
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
MATSUKI MAYUMI
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
KATO TOSHIYUKI
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
NAKAJIMA HIROSHI
(Japan Advanced Inst. Sci. and Technol., Hokuriku)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.16th;NO.;PAGE.18-19(2001)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;HemAT that is a putative oxygen sensing heme protein for aerotaxis of Bacillus subtilis. In this study, we have constructed an expression system of HemAT and purified the recombinant HemAT to characterize its molecular properties. The recombinant HemAT was expressed as a soluble protein in E. coli. HemAT as isolated showed a typical uv/vis spectrum for six-coordinate, low-spin hemeproteins, which was similar to that of the oxy form of myoglobin. When HemAT as isolated was reacted with CO, the CO-bound form was formed. A typical uv/vis spectrum for five-coordinate, high-spin hemeproteins was observed upon the reaction of the isolated HemAT with sodium dithionite, which is similar to that of the deoxy form of myoglobin. These results suggest that HemAT has been purified as the oxygen-bound(oxy) form. Resonance Raman spectroscopy has revealed that HemAT as isolated is indeed in the oxy form. We will discuss the environmental structure around the heme in HemAT that has been elucidated by site-directed mutagenesis. (author abst.) |
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