The chemistry and biochemistry of heme c: functional bases for covalent attachment.
A discussion of the literature concerning the synthesis, function, and activity of heme c-containing proteins is presented. Comparison of the properties of heme c, which is covalently bound to protein, is made to heme b, which is bound noncovalently. A question of interest is why nature uses biochemically expensive heme c in many proteins when its properties are expected to be similar to heme b. Considering the effects of covalent heme attachment on heme conformation and on the proximal histidine interaction with iron, it is proposed that heme attachment influences both heme reduction potential and ligand-iron interactions.
Bowman
Sarah E J
SE
Department of Chemistry, University of Rochester, Rochester, NY 14627, USA.
Bren
Kara L
KL
D006418:Heme / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D006639:Histidine / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure
C031690:heme C; D006418:Heme; D006639:Histidine