✦ LIBER ✦

Redox Properties of Cytochrome c Adsorbed on Self-Assembled Monolayers: A Probe for Protein Conformation and Orientation

✍ Scribed by Chen, Xiaoxi; Ferrigno, Rosaria; Yang, Jerry; Whitesides, George M.

Book ID: 121876420
Publisher: American Chemical Society
Year: 2002
Tongue: English
Weight: 171 KB
Volume: 18
Category: Article
ISSN: 0743-7463
DOI: 10.1021/la0204794

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Molecular Simulation Studies of the Orie

Molecular Simulation Studies of the Orientation and Conformation of Cytochrome c Adsorbed on Self-Assembled Monolayers

✍ Zhou, Jian; Zheng, Jie; Jiang, Shaoyi 📂 Article 📅 2004 🏛 American Chemical Society 🌐 English ⚖ 459 KB

Probing the Conformation and Orientation

Probing the Conformation and Orientation of Adsorbed Protein Using Monoclonal Antibodies: Cytochrome c 3 Films on a Mercury Electrode

✍ Egodage, Kamal L.; de Silva, Binodh S.; Wilson, George S. 📂 Article 📅 1997 🏛 American Chemical Society 🌐 English ⚖ 177 KB

Characterization and redox properties of

Characterization and redox properties of cytochrome c552 from Thermus thermophilus adsorbed on different self-assembled thiol monolayers, used to model the chemical environment of the redox partner

✍ Sophie Bernad; Tewfik Soulimane; Zineb Mehkalif; Sophie Lecomte 📂 Article 📅 2006 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 385 KB 👁 1 views

## 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

Self-assembled monolayers of mercaptosuc

Self-assembled monolayers of mercaptosuccinic acid monolayers on silver and gold surfaces designed for protein binding. Part II: vibrational spectroscopy studies on cytochrome c immobilization

✍ Agata Królikowska; Jolanta Bukowska 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 235 KB

Redox and conformational equilibria of c

Redox and conformational equilibria of cytochrome c552 from Thermus thermophilus adsorbed on a chemically modified silver electrode probed by surface-enhanced resonance Raman spectroscopy

✍ Sophie Bernad; Tewfik Soulimane; Sophie Lecomte 📂 Article 📅 2004 🏛 John Wiley and Sons 🌐 English ⚖ 291 KB

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