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| Content Provider | PubMed Central |
|---|---|
| Author | Morleo, Anna Bonomi, Francesco Iametti, Stefania Huang, Victor W. Kurtz, Donald M. |
| Abstract | Addition of iron salts to chaotrope-denatured aporubredoxin (apoRd) leads to nearly quantitative recovery of its single Fe(SCys)4 site and native protein structure without significant dilution of the chaotrope. This “high chaotrope” approach was used to examine iron binding and protein folding events using stopped-flow UV/vis absorption and CD spectroscopies. At 100-fold molar excess ferrous iron over denatured apoRd maintained in 5 M urea, the folded holoFeIIIRd structure was recovered in >90% yield with t 1/2 < 10 msec. More modest excesses of iron also gave nearly quantitative holoRd formation in 5 M urea but with chronological resolution of iron binding and protein folding events. The results indicate structural recovery in 5 M urea consists of the minimal sequence: (1) binding of ferrous iron to the unfolded apoRd, (2) rapid formation of a near-native ferrous Fe(SCys)4 site within a protein having no detectable secondary structure, (3) recovery of the ferrous Fe(SCys)4 site chiral environment nearly concomitantly with (4) recovery of the native protein secondary structure. The rate of step 2 (and by inference, step 1) was not saturated even at 100-fold molar excess of iron. Analogous results obtained on Cys→Ser iron ligand variants support formation of an unfolded-Fe(SCys)3 complex between steps 1 and 2, which we propose is the key nucleation event that pulls distal regions of the protein chain together. These results show that folding of chaotrope-denatured apoRd is iron-nucleated and driven by extraordinarily rapid formation of the Fe(SCys)4 site from an essentially random coil apoprotein. This high chaotrope, multi-spectroscopic approach could clarify folding pathways of other [M(SCys)3 or 4]-containing proteins. |
| Related Links | http://dx.doi.org/10.1021/bi100630t |
| Ending Page | 6634 |
| Page Count | 8 |
| Starting Page | 6627 |
| File Format | |
| ISSN | 00062960 |
| e-ISSN | 15204995 |
| Journal | Biochemistry |
| Issue Number | 31 |
| Volume Number | 49 |
| Language | English |
| Publisher Date | 2010-08-10 |
| Access Restriction | Open |
| Subject Keyword | Biochemistry Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry |
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