Sandbox Reserved 335: Difference between revisions
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All members in the C-type cytochrome superfamily contain a heme prosthetic group that is covalently attached to the protein via two thioether bonds to cysteine residues.<ref name=main>PMID:18855424</ref> Most cytochromes ''c'' occur in a CXXCH motif, where a histidine residue is one of the two axial ligands of the heme iron. The other axial position may be left vacant or be occupied mostly by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main /> | All members in the C-type cytochrome superfamily contain a heme prosthetic group that is covalently attached to the protein via two thioether bonds to cysteine residues.<ref name=main>PMID:18855424</ref> Most cytochromes ''c'' occur in a CXXCH motif, where a histidine residue is one of the two axial ligands of the heme iron. The other axial position may be left vacant or be occupied mostly by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main /> | ||
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== Mechanism == | == Mechanism == | ||
