Title : Metabolism-based covalent bonding of the heme prosthetic group to its apoprotein during the reductive debromination of BrCCl3 by myoglobin.

Pub. Date : 1990 Jun 25

PMID : 2355004






5 Functional Relationships(s)
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Protein Name
Organism
1 It was found that the prosthetic heme was modified by a CCl2 moiety derived from BrCCl3 and was covalently bound to histidine residue 93, the normal proximal ligand to the heme-iron. Heme C-C motif chemokine ligand 2 Homo sapiens
2 It was found that the prosthetic heme was modified by a CCl2 moiety derived from BrCCl3 and was covalently bound to histidine residue 93, the normal proximal ligand to the heme-iron. Bromotrichloromethane C-C motif chemokine ligand 2 Homo sapiens
3 It was found that the prosthetic heme was modified by a CCl2 moiety derived from BrCCl3 and was covalently bound to histidine residue 93, the normal proximal ligand to the heme-iron. Histidine C-C motif chemokine ligand 2 Homo sapiens
4 It was found that the prosthetic heme was modified by a CCl2 moiety derived from BrCCl3 and was covalently bound to histidine residue 93, the normal proximal ligand to the heme-iron. Heme C-C motif chemokine ligand 2 Homo sapiens
5 It was found that the prosthetic heme was modified by a CCl2 moiety derived from BrCCl3 and was covalently bound to histidine residue 93, the normal proximal ligand to the heme-iron. Iron C-C motif chemokine ligand 2 Homo sapiens