Transient complexes of redox proteins: structural and dynamic details from NMR studies

• Published in: Journal of molecular recognition 2004-11, Vol.17 (6), p.524-539
• Main Authors: Prudêncio, Miguel, Ubbink, Marcellus
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; cytochromes; Cytochromes - chemistry; Cytochromes - metabolism; electron transfer; electrostatic; flavin proteins; Fungal Proteins - chemistry; Fungal Proteins - metabolism; hydrophobic; iron-sulphur proteins; Magnetic Resonance Spectroscopy; Multiprotein Complexes - chemistry; Oxidation-Reduction; Protein Binding; Protein Conformation; redox enzyme
• ISSN: 0952-3499; 1099-1352
• DOI: 10.1002/jmr.686

Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Protein–protein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Two‐dimensional NMR spectroscopy has been applied to many redox protein complexes, providing a wealth of information about the process of complex formation, the nature of the interface and the dynamic properties of the complex. These studies have shown that some complexes are non‐specific and exist as a dynamic ensemble of orientations while in other complexes the proteins assume a single orientation. The binding interface in these complexes consists of a small hydrophobic patch for specificity, surrounded by polar, uncharged residues that may enhance dissociation, and, in most complexes, a ring or patch of charged residues that enhances the association by electrostatic interactions. The entry and exit port of the electrons is located within the hydrophobic interaction site, ensuring rapid electron transfer from one redox centre to the next. Copyright © 2004 John Wiley & Sons, Ltd.