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[__ Science __ ] Hemoglobin: An Exquisitely Designed, Multifunctional Protein

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When we begin to examine life on the molecular level, we quickly begin to realize that hemoglobin is specially designed for multiple purposes.

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Actually, hemoglobin is a fairly late arrival, being a modified molecule made up of heme subunits around an iron-bearing molecule. Heme existed prior to the evolution of hemoglobin:

Evolving Genes and Proteins
A Symposium Held at the Institute of Microbiology of Rutgers: the State University with Support from the National Science Foundation
Evolution of Heme and Chlorophyll
S.GRANICK
This chapter discusses the evolution of heme and chlorophyll. Heme and chlorophyll are not only the two end products of the same biosynthetic chain but are also related in function. Heme serves as a catalyst for respiration to release the energy stored in organic bonds. Chlorophyll serves as a catalyst to convert the energy of sunlight into the stored chemical energy of organic bonds. The basic energetics of protoplasm is catalyzed by these two pigments derived from the same biosynthetic chain. The functions of respiration and photosynthesis in protoplasm provide energy for maintenance and renewal. The chapter presents some hypotheses on how these functions may have been accomplished in a primitive form in inorganic mineral catalysts, how organic molecules came to take over these functions, and how these organic molecules were modified as the biosynthetic chains developed.
 
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