Rieske Protein
Rieske proteins are iron-sulfur protein (ISP) components of cytochrome bc1 complexes and cytochrome b6f complexes which were first discovered and isolated by John S. Rieske and co-workers in 1964. It is a unique cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria with widely ranging electron reduction potentials from -150 to +400 mV.
Read more about Rieske Protein: Biological Function (in Oxidative Phosphorylation Systems), Rieske Protein Family, 3D Structure, Subfamilies, Human Proteins Containing This Domain
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