Complete Thermodynamic Characterization of Reduction and Protonation of the bc1-type Rieske [2Fe-2S] Center of Thermus thermophilus
Author:
Affiliation:
1. Medical Research Council Dunn Human Nutrition Unit, Hills Road Cambridge, CB2 2XY, U.K. Department of Biology University of California at San Diego La Jolla, California 92093
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja016532c
Reference20 articles.
1. Electron-nuclear double resonance spectroscopy of nitrogen-15-enriched phthalate dioxygenase from Pseudomonas cepacia proves that two histidines are coordinated to the [2Fe-2S] Rieske-type clusters
2. Structure of a water soluble fragment of the ‘Rieske’ iron–sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 å resolution
3. Structure and Function of Cytochrome bc Complexes
4. Active Site Structure of Rieske-Type Proteins: Electron Nuclear Double Resonance Studies of Isotopically Labeled Phthalate Dioxygenase from Pseudomonas cepacia and Rieske Protein from Rhodobacter capsulatus and Molecular Modeling Studies of a Rieske Center,
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