Hemoglobin structure and synthesis

Necheles, T. F. Allen, D. M. Finkel, H. E., "Clinical Disorders of Hemoglobin Structure and Synthesis", Appleton-Century-Crofts, N.Y., 1969. 

SECTION 28.3 Inherited Disorders of Hemoglobin Structure and Synthesis... 

Necheles T, Allen D, Finkel M (1969) Clinical disorders of hemoglobin structure and synthesis. Academic Press, London New York Nelson O (1968) Genetics 60 507-524... 

Streptomyces distallicus the structure elucidation and synthesis have also been made by them.165 A wide variety of porphyrins which are derivatives of porphin (125 R = H) occur in nature and exert three biological functions (a) oxygen storage and transport, as in hemoglobin, (b) cellular respiration as in the cytochromes, and (c) photosynthesis, as in the chlorophylls for detailed discussion of structures and synthesis of naturally occurring porphyrins, see references.166 Recent developments in the chemistry of polypyrrolic compounds have been reviewed.167 Several naturally occurring indole alkaloids have dimeric structures of type B,168 an example of which is c-toxiferine-I, a calabash curare alkaloid found in South American species of Strychnos.169... 

RNA secondary structure plays a role in the regulation of iron metabolism in eukaryotes. Iron is an essential nutrient, required for the synthesis of hemoglobin, cytochromes, and many other proteins. However, excess iron can be quite harmful because, untamed by a suitable protein environment, iron can initiate a range of free-radical reactions that damage proteins, lipids, and nucleic acids. Animals have evolved sophisticated systems for the accumulation of iron in times of scarcity and for the safe storage of excess iron for later use. Key proteins include transferrin, a transport protein that carries iron in the serum, transferrin receptor, a membrane protein that binds iron-loaded transferrin and initiates its entry into cells, and ferritin, an impressively efficient iron-storage protein found primarily in the liver and kidneys. Twenty-four ferritin polypeptides form a nearly spherical shell that encloses as many as 2400 iron atoms, a ratio of one iron atom per amino acid (Figure 31.37). 

This book provides an overview of possible combinations of metal complexes and metals with organic and inorganic macromolecules (often also named macromolecular metal complexes — MMC [1]). This book covers the formation, synthesis, structure and properties of these exciting and relatively new materials. Metal-containing macromolecules are a fascinating field of science. It is readily understandable that materials with unusual properties are obtained by having a metal complex or metal as part of a macromolecule. Nature shows us the functions of such materials extremely well by the selectivity and activity of, for example, hemoglobin, photosynthesis and metalloenzymes. 

The first chemical synthesis of a natural protein was also that of insulin. Furthermore, the first three-dimensional protein structures determined were those of myoglobin, the oxygen storage/transport protein of muscle, and hemoglobin, the structurally related oxygen transport protein of blood. The structure and function of hemoglobins are considered in Chapter 7. 

Methods for the synthesis of pyrroles are of importance, since the pyrrole unit is found in natural products widespread in nature. For example a pyrrole unit is the building block of the porphyrin skeleton, which in turn is the essential structural subunit of chlorophyll and hemoglobin. 

---