The terminal caa 3 oxidase of Thermus thermophilus has been studied by resonance Raman spectroscopy. Using different excitation wavelengths in the Soret band region, it was possible to disentangle the resonance Raman spectra of the fully oxidized and fully reduced state in terms of the component spe
Magnetization Studies of the Reduced Active Form of the Catalase from Thermus thermophilus
✍ Scribed by Lilian Jacquamet; Dr. Isabelle Michaud-Soret; Dr. Noële Debaecker-Petit; Dr. Jean-Marc Latour; Dr. Vladimir V. Barynin; Dr. Jean-Luc Zimmermann
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 404 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0044-8249
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The ba 3 cytochrome oxidase from Thermus thermophilus was studied by resonance Raman spectroscopy. The component spectra of both heme groups were determined by using different excitation wavelengths. In the ferric state the heme a 3 group reveals resonance Raman marker bands characteristic for two h
The aim of this paper is to test the ability of a β-glycosidase regioselectivity of the reactions is mainly of the β-[1Ǟ3] type, good yields are obtained for the synthesis of 2-nitrophenyl-from Thermus thermophilus to catalyse transglycosylation reactions in the presence of nitrophenyl glycosides as
## Abstract The structure of cytochrome __c~552~__ (Cyt‐__c~552~__) from __Thermus thermophilus__ shows many differences to other __c‐__type cytochromes. The rich lysine domain close to the heme does not exist in this cytochrome, allowing us to postulate that the interaction with its redox partner