Stopped-flow spectrophotometric and resonance Raman analyses of aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis
| Autor: | Michihiko Kobayashi, Teizo Kitagawa, Kazunobu Konishi, Takehiro Ohta, Hiroki Higashibata, Ken-Ichi Oinuma, Yoshitsugu Shiro, Hideyuki Kumita, Yoshiteru Hashimoto |
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| Rok vydání: | 2004 |
| Předmět: |
inorganic chemicals
Hemeprotein Nitrogen Resonance Raman spectroscopy Biophysics Heme Reaction intermediate Photochemistry Spectrum Analysis Raman Biochemistry Catalysis Ferrous symbols.namesake chemistry.chemical_compound Structural Biology Genetics Histidine Stopped-flow spectrophotometry Molecular Biology Hydro-Lyases Isosbestic point Dehydration Molecular Structure Spectrum Analysis Cell Biology Triple bond Carbon Kinetics chemistry Mutation symbols Raman spectroscopy Nitrile |
| Zdroj: | FEBS letters. 579(6) |
| ISSN: | 0014-5793 |
| Popis: | On stopped-flow analysis of aliphatic aldoxime dehydratase (OxdA), a novel hemoprotein, a spectrum derived from a reaction intermediate was detected on mixing ferrous OxdA with butyraldoxime; it gradually changed into that of ferrous OxdA with an isosbestic point at 421nm. The spectral change on the addition of butyraldoxime to the ferrous H320A mutant showed the formation of a substrate-coordinated mutant, the absorption spectrum of which closely resembled that of the above intermediate. These observations and the resonance Raman investigation revealed that the substrate actually binds to the heme in OxdA, forming a hexa-coordinate low-spin heme. |
| Databáze: | OpenAIRE |
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