CHE 350 Lecture Notes - Lecture 5: Myoglobin, Cytoglobin, Neuroglobin
Document Summary
Ch 7-1 (pp 180 200: myoglobin and hemoglobin (both reversibly bind molecular oxygen, myoglobin: small, simple protein. Intracellular protein in vertebrate muscle: most residues are in 8 helices, form globular protein, contains heme prosthetic group. +[2] as well as yo2 = 2+2 (partial pressure: the fraction of o2-binding sites occupied by o2, ranges from 0 to 1, by combining with the dissociation constant (kd), you get: Lower po2: little o2 binds to myoglobin (yo2 is small: higher po2: more o2 binds to myoglobin (at very high po2, the myoglobin is saturated with o2) I(cid:374) t state, his (cid:1013)(cid:1011) i(cid:374) the (cid:272)hai(cid:374) (cid:272)o(cid:374)ta(cid:272)ts th(cid:396) 41 i(cid:374) the (cid:272)hai(cid:374), i(cid:374) the r state, His 97 contacts thr 38: c-terminal residues of each subunit form ion pairs the stabilize the t state but are torn apart in t r transition due to the energy formation of the fe- Binding one o2 changes the conformation from t to.
