Surface-enhanced resonance Raman (SERR) spectroscopy was employed to study the potential-dependent processes of the electron-transferring heme protein cytochrome of Thermus thermophilus adsorbed on a silver c 552 (Cyt-c 552 ) electrode. In the reduced state, the SERR spectrum of is very similar to t
Engineering of Thermus thermophilus Cytochrome c552: Thermally Tolerant Artificial Peroxidase*
โ Scribed by Hiroshi Nakajima; Yusuke Ichikawa; Yuh Satake; Nobuyuki Takatani; Soumen Kanti Manna; Jitumani Rajbongshi; Shyamalava Mazumdar; Yoshihito Watanabe
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 197 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1439-4227
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๐ SIMILAR VOLUMES
Surface-enhanced resonance Raman spectroscopy (SERRS) was employed to study the potential-dependent processes of the electron transferring heme protein cytochrome c 552 (Cyt-c 522 ) from Thermus thermophilus. Cyt-c 552 was adsorbed on Ag electrodes coated with functionalized self-assembled monolayer
## Abstract The structure of cytochrome __c~552~__ (Cytโ__c~552~__) from __Thermus thermophilus__ shows many differences to other __cโ__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