Isolation, Characterisation and Crystallisation of a Water-Soluble Fragment of the Rieske Iron-Sulfur Protein of Bovine Heart Mitochondrial bc1 Complex
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.0071n.x/fullpdf
Reference38 articles.
1. The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex.
2. Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske iron-sulfur centers of the cytochrome b6f complex on spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaeroides R-26, and bovine heart mitochondria
3. A computerized calibration of the circular dichrometer
4. Circular dichroic analysis of protein conformation: Inclusion of the β-turns
5. Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas.
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