Jones, Kathryn and Gomes, Claudio M. and Huber, Harald and Teixeira, Miguel and Wittung-Stafshede, Pernilla (2002) Formation of a linear [3Fe-4S] cluster in a seven-iron ferredoxin triggered by polypeptide unfolding. JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 7 (4-5). pp. 357-362. ISSN 0949-8257
Full text not available from this repository. (Request a copy)Abstract
Cubic iron-sulfur ([Fe-S]) clusters are common inorganic cofactors in proteins. The presence of a linear [3Fe-4S] cluster in a protein was first observed in beef-heart aconitase at high pH, where the protein structure was perturbed. Not long ago, the same linear cluster was discovered upon unfolding of a thermophilic di-cluster seven-iron ferredoxin, suggesting a more general relevance for this type of linear clusters in Nature. Since structure-induced cluster rearrangements may be important regulatory, on-going processes in living systems, we decided to further characterize the formation of the linear iron-sulfur cluster observed upon ferredoxin unfolding. Here we present a kinetic investigation of parameters that affect the linear-cluster formation and disassembly in the Sulfolobus acidocaldarius seven-iron ferredoxin. We find the linear cluster to be an intermediate on the protein-mediated cluster-degradation pathway under a wide range of pH and denaturant conditions. The linear species forms in parallel with secondary-structure disappearance. In contrast, the disassembly rate constant for the linear cluster is independent of denaturant concentration but depends strongly on solution pH. At high pH, the disassembly rate is slower and the linear iron-sulfur species has a longer lifetime, than at low pH.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEINS; AMBIVALENS; iron-sulfur proteins; protein unfolding; cluster degradation; kinetics; mechanism |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Nov 2021 14:07 |
| Last Modified: | 02 Nov 2021 14:07 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40425 |
Actions (login required)
 |
View Item |
