Source:http://linkedlifedata.com/resource/pubmed/id/11821422
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
16
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| pubmed:dateCreated |
2002-4-15
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| pubmed:abstractText |
HemAT-Bs is a heme-containing signal transducer protein responsible for aerotaxis of Bacillus subtilis. The recombinant HemAT-Bs expressed in Escherichia coli was purified as the oxy form in which oxygen was bound to the ferrous heme. Oxygen binding and dissociation rate constants were determined to be k(on) = 32 microm(-1) s(-1) and k(off) = 23 s(-1), respectively, revealing that HemAT-Bs has a moderate oxygen affinity similar to that of sperm whale myoglobin (Mb). The rate constant for autoxidation at 37 degrees C was 0.06 h(-1), which is also close to that of Mb. Although the electronic absorption spectra of HemAT-Bs were similar to those of Mb, HemAT-Bs showed some unique characteristics in its resonance Raman spectra. Oxygen-bound HemAT-Bs gave the nu(Fe-O(2)) band at a noticeably low frequency (560 cm(-1)), which suggests a unique hydrogen bonding between a distal amino acid residue and the proximal atom of the bound oxygen molecule. Deoxy HemAT-Bs gave the nu(Fe-His) band at a higher frequency (225 cm(-1)) than those of ordinary His-coordinated deoxy heme proteins. CO-bound HemAT-Bs gave the nu(Fe-CO) and nu(C-O) bands at 494 and 1964 cm(-1), respectively, which fall on the same nu(C-O) versus nu(Fe-CO) correlation line as that of Mb. Based on these results, the structural and functional properties of HemAT-Bs are discussed.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/heme protein, bacteria
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
19
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| pubmed:volume |
277
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
13528-38
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11821422-Amino Acid Sequence,
pubmed-meshheading:11821422-Bacillus subtilis,
pubmed-meshheading:11821422-Bacterial Proteins,
pubmed-meshheading:11821422-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11821422-Escherichia coli,
pubmed-meshheading:11821422-Heme,
pubmed-meshheading:11821422-Hemeproteins,
pubmed-meshheading:11821422-Hydrogen,
pubmed-meshheading:11821422-Hydrogen-Ion Concentration,
pubmed-meshheading:11821422-Isotopes,
pubmed-meshheading:11821422-Kinetics,
pubmed-meshheading:11821422-Ligands,
pubmed-meshheading:11821422-Molecular Sequence Data,
pubmed-meshheading:11821422-Oxygen,
pubmed-meshheading:11821422-Protein Binding,
pubmed-meshheading:11821422-Protein Structure, Tertiary,
pubmed-meshheading:11821422-Recombinant Proteins,
pubmed-meshheading:11821422-Signal Transduction,
pubmed-meshheading:11821422-Spectrum Analysis, Raman,
pubmed-meshheading:11821422-Ultraviolet Rays
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| pubmed:year |
2002
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| pubmed:articleTitle |
Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis.
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| pubmed:affiliation |
School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Ishikawa, Japan. aono@jaist.ac.jp
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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