Biochemistry Glossary Hemoglobin Myoglobin 4 Dissociation Curves The highest levels of expression of myoglobin are in the heart. hemoglobin. adult hemoglobin is a [α(2):β(2)] tetrameric hemeprotein found in erythrocytes where it is responsible for binding oxygen in the lung and transporting the bound oxygen throughout the body where it is used in aerobic metabolic pathways. structure of hemoglobin. The o 2 pressure at which half of the molecules in a solution of myoglobin are bound to o 2 (p 1 2) is about 1 mm hg (1.3 × 10 −3 atm). figure 4.2.2: oxygen binding to myoglobin and hemoglobin. (a) the fe 2 ion in deoxymyoglobin is high spin, which makes it too large to fit into the “hole” in the center of the porphyrin.
Biochemistry Glossary Hemoglobin Myoglobin 1 Heme Group Draw It This page titled 4.1: myoglobin, hemoglobin, and their ligands is shared under a cc by nc sa 4.0 license and was authored, remixed, and or curated by henry jakubowski. hemoglobin and myoglobin have played important roles in the history of biochemistry. they were the first proteins for which three dimensional structures were determined by x ray. Myoglobin is a protein located primarily in the striated muscles of vertebrates. mb is the gene encoding myoglobin in humans. it encodes a single polypeptide chain with one oxygen binding site. myoglobin contains a heme prosthetic group that can reversibly bind to oxygen. the body uses it as an oxygen storage protein in muscle. it is able to bind and release oxygen depending on the oxygen. Biochemistry 29:1515–1523. 10.1021 bi00458a024 [google scholar] lokich jj, moloney wc, bunn hf et al. (1973) hemoglobin brigham (alpha2abeta2100 pro–leu). hemoglobin variant associated with familial erythrocytosis. j clin invest 52:2060–2067. 10.1172 jci107390 [pmc free article] [google scholar]. Almost all biochemistry textbooks start their description of the biological functions of proteins using the myoglobin and hemoglobin as exemplars. these are very rational approaches since they have become model systems to describe the binding of simple ligands, like dioxygen (o2), co2, and h , and how the structure of the protein determines and is influenced by binding of ligands.
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