Cytochrome b(562) folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein

Citation
P. Wittung-stafshede et al., Cytochrome b(562) folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein, P NAS US, 96(12), 1999, pp. 6587-6590
Citations number
42
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN journal
00278424 → ACNP
Volume
96
Issue
12
Year of publication
1999
Pages
6587 - 6590
Database
ISI
SICI code
0027-8424(19990608)96:12<6587:CBFTBE>2.0.ZU;2-9
Abstract
Ferrocytochrome b(562) [Fe(II)cyt b(562)] folding can be triggered by photo induced electron transfer to unfolded Fe (III)cyt b(562) in 2-3 M guanidine hydrochloride solutions, The folding rates increase with decreasing guanid ine hydrochloride; the extrapolated time constant for this folding process in the absence of denaturant (5 mu s) is near the predicted value for intra chain diffusion. The relatively smooth energy landscape indicated for Fe(II )cyt b(562) folding accords with the helical, highly symmetrical structure of the protein.