BCH 369 Lecture Notes - Lecture 5: Heme, Myoglobin, Dissociation Constant
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4 peptide chains and 4 heme is a tetramer with groups. 213 held together by salt bridges and h bonding hemoglobinexists in. Theheme in tstate is tightly bound oz binding causestheheme planeto flatten. Hemoglobin binds 02 inlungs butrelease intissue whereo2 is needed metabolism a large fraction ofits 0. In blood hemoglobin mostly nhst 99 but nhz 11 aminogroups of hemo good t egt . Coz theco2 istransported to lungs and released go. fm e. High co2concentration and carbamate formation promotes oz release from hemoglobin. I hc05 ht pka i 6 s at. Reaction found in redbloodcells catalited by carbonic anhydrase an enzyme pka. Same 2x as adult but 2 different 13. Fetal hemoglobin hashigher affinity for oz than mother"s regular hemoglobin. Facilitates 02 transfer tofrom mother to fetus in placenta. Sickle cell anemia mutation in hemoglobin single aa change glo ual results in fiber formation inside red blood cells distortingcellshape.
