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
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.