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Updated: Jul 22, 2026

Antigens Protected Functional Red Blood Cells By The Membrane Grafting Of Compact Hyperbranched Polyglycerols
Published on: January 2, 2013
Unusual heme-histidine bond in the active site of a chaperone
Donghan Lee1, Konstantin Pervushin, Daniela Bischof
1Laboratory of Physical Chemistry and Institute of Microbiology, ETH Hönggerberg, CH-8093 Zürich, Switzerland.
Abstract:
The heme chaperone CcmE is essential for the delivery of heme to c-type cytochromes. It forms an unusual transient, yet covalent, bond between an essential histidine, H130, and heme. We report on the discovery of the chemical structure of this bond solved by NMR, where the heme vinyl is cross-linked at the beta carbon to the Ndelta1 of H130. As this type of heme linkage has not been described previously in any cytochrome or hemoprotein, it represents a novel type of heme-histidine complex.
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