Hemoglobin evolution

R. E. Dickerson and I. Geis, Hemoglobin Structure, Tunction, Evolution andPathology, Benjamin/Cummings, Menlo Park, Calif., 1983. 

Dickerson, R. E., and Geis, I., 1983. Hemoglobin Structure, Function, Evolution and Pathology. Menlo Park, CA Benjamin/Cnmming.s. 

Manz, B Stilbs, P Jonsson, B Soderman, O Callaghan, PT, NMR Imaging of the Time Evolution of Electroosmotic Flow in a Capillary, Journal of Physical Chemistry 99, 11297, 1995. Matthew, JB Hanania, GIH Gurd, FRN, Electrostatic Effects in Hemoglobin Bohr Effect and Ionic Strength Dependence of Individual Groups, Biochemistry 18, 1928, 1979. 

In this report we would like to discuss our results on the picosecond photodissociation experiments of the CO and O2 forms of a number of synthetic reversible oxygen carriers (1,2) and compared them to earlier picosecond absorption work on the same derivatives of the natural forms of hemoglobin. The latter work has provided us with a better understanding of the details of the photodissociation in terms of the sequential evolution of four photointermediates which were experimentally isolated, characterized, and kinetically analyzed (3,4). 

The parallels and differences among hemoglobin, hemerylhrm. and hemocyamn illustrate the ways in which evolution has often solved what is basically the same problem in different ways in different groups of animals.51... 

The amino acid sequences of hemoglobins have been extensively altered hy mutation during evolution Data on the umino acid sequences ol the chains from a vanetv of mamma Ii.hi and mliei veiiebruie hemoglobins show thai the sequence can be varied extensively wilhoui drastic change... 

The suggested relationship between numbers ol differences and evolutionary lime is not wholly secure. It assumes uniformity in the tale of clleeiive amino acid substitution, but this rale mas he neither iindorm with time, nor uniform in different pails of the polv vpticle chain. Differences in the rate of effective substitution along Ihe polypeptide chain may be due not only 10 restrictions imposed by the required tertiary structure, hut also to differences in the rate at which various parts of tile l).NA or the gene mutate. The evolution of hemoglobin mav he contrasted w ith that of cytochrome e in which approximately 500 of the molecule appears io have remained invariant purine the lime yeast arid man have evolved. 

Hardison, R. (1998). Hemoglobins from bacteria to man evolution of different patterns of gene expression. J. Exp. Biol. 201 1099-1117. 

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