| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1317084 | Journal of Inorganic Biochemistry | 2007 | 8 Pages |
Abstract
The folding kinetics of R. palustris cytochrome c′ (cyt c′) have been monitored by heme absorption and native Trp72 fluorescence at pH 5. The Trp72 fluorescence burst signal suggests early compaction of the polypeptide ensemble. Analysis of heme transient absorption spectra reveals deviations from two-state behavior, including a prominent slow phase that is accelerated by the prolyl isomerase cyclophilin. A nonnative proline configuration (Pro21) likely interferes with the formation of the helical bundle surrounding the heme.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Ekaterina V. Pletneva, Ziqing Zhao, Tetsunari Kimura, Krastina V. Petrova, Harry B. Gray, Jay R. Winkler,