BIOC 3560 Lecture Notes - Lecture 2: Royal Aircraft Factory F.E.2, Heme, Myoglobin
28 Nov 2015
School
Department
Course
Professor
Document Summary
A volunteer note taker has been requested for this course by the centre for students with disabilities. Anyone interested in helping a fellow student is asked to drop by the csd office, rm 318b u. c. For more information, call extension 52073 or e-mail [email protected] ca. Volunteer forms are available at the office or on the csd website: http://www. uoguelph. ca/csd/ O2 is complexed with transition metals that have high affinities for o2 e. g. iron and copper. Free iron can promote the formation of highly reactive o2 species. This tendency is reduced when iron is incorporated into heme heme: a prosthetic group. Substitutions at x" (e. g. propionate in heme) 4 n atoms that can bond with fe2+ heme: fe2+ binds o2 reversibly, fe3+ does not bind o2. In heme-containing proteins, irreversible oxidation of fe2+ by. O2 is prevented: heme is buried within the protein, one coordination bond is occupied by a side-chain n of a his residue, o2 binds reversibly at remaining position.
