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Cytochrome c'β-Met Is a Variant in the P460 Superfamily Lacking the Heme-Lysyl Cross-Link: A Peroxidase Mimic Generating a Ferryl Intermediate.

Biochemistry. 2020-02; 
Liew FN, Brandys MA, Biswas S, Nguyen JN, Rahmawati M, Nevala M,, Elmore BO, Hendrich MP, Kim HJ.
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PCR Cloning and Subcloning … for heme using the TMBZ-H2O2 peroxidase activity method22 Construction of Clones and Growth Conditions The genes encoding cytochrome c′β-Met was cloned by GenScript Corp into a pET-20(b+) plasmid in frame with the plasmid's N-terminal Page 6 of 39 … Get A Quote

摘要

A defining characteristic of bacterial cytochromes (cyt's) in the P460 family is an unusual cross-link connecting the heme porphyrin to the side chain of a lysyl residue in the protein backbone. Here, via proteomics of the periplasmic fraction of the ammonia-oxidizing bacterium (AOB) Nitrosomonas europaea, we report the identification of a variant member of the P460 family that contains a methionyl residue in place of the cross-linking lysine. We formally designate this protein cytochrome "c'β-Met" to distinguish it from other members bearing different residues at this position (e.g., cyt c'β-Phe from the methane-oxidizing Methylococcus capsulatus Bath). As isolated, the monoheme cyt c'β-Met is high-spin (S ... More

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