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Cytochrome b562 is a small, soluble heme-containing protein primarily found in the periplasmic space of Gram-negative bacteria such as Escherichia coli. [1] It is structurally defined by a characteristic four-helix bundle fold that non-covalently coordinates a single heme b prosthetic group through axial ligation with Methionine-7 and Histidine-102. [2] Biologically, the protein acts as an electron transfer agent within the bacterial cell, although its specific physiological redox partners are not fully established. [3] Due to its high conformational stability, simple architecture, and well-characterized biophysical properties, cytochrome b562 has become a premier model system for studying protein folding kinetics and de novo protein design. [4] Researchers frequently utilize it as a structural scaffold for engineering novel metalloenzymes and biosensors. [5] Currently, cytochrome b562 is not recognized as a therapeutic target for human disease, and there are no approved or experimental drugs known to interact with it for clinical purposes. [6]
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