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each case. We can only stand amazed at how the<br />

Creator solved this problem, which is why it is<br />

worth giving a little more detail:<br />

Carrying out these specific functions requires an<br />

extraordinarily ingenious molecular construction.<br />

It is the hemoglobin molecule (Hb), which chemically<br />

is a tetrameric iron protein. It consists of a<br />

globin molecule and four heme molecules. Globin<br />

consists of four subunits, namely four long<br />

protein chains (two lots of identical type, i.e. two<br />

pairs). A heme molecule is attached to each of<br />

these chains such that the four heme units lie in<br />

“pouches” close to the surface of the entire Hb<br />

molecule. Heme is a ringshaped molecule, which<br />

contains an iron atom at its centre. Hb consists<br />

of 0.334% iron; the total quantity of iron in the<br />

blood is about 3 grams, or 70% of the iron in the<br />

entire human body.<br />

Protein molecules consist of long chains of various<br />

amino acids, and undergo folding after they<br />

have been assembled. The characteristic threedimensional<br />

structure each protein adopts, which<br />

gives it its function, depends on the types and<br />

sequence of these amino acids. If just a few<br />

(depending on the position, even one) of these<br />

amino acids are substituted by others, or amino<br />

acids are added or omitted, the entire geometry<br />

of the molecule is affected, and thus also its<br />

capacity for gas transport.<br />

62<br />

a) In the adult stage (here regarded as commencing<br />

at birth), our blood contains exactly that<br />

hemoglobin (HbA = adult) in which the four protein<br />

chains are constructed so as to give the<br />

entire molecule the precise affinity for oxygen<br />

needed for us to live. HbA has two each of the<br />

already mentioned α und β protein chains. The<br />

chemical structure of these chains must be very<br />

precise, or else severe diseases (anemias) will<br />

result. For instance, sickle cell anemia has arisen<br />

through mutation causing just one single amino<br />

acid residue in the β chain to be replaced by<br />

another. Even this minuscule change results in<br />

an aberrant, pathological form of Hb. We can see<br />

here that the sort of tinkering and experimentation<br />

with amino acid sequences that evolutionary<br />

thinking requires is largely ruled out. The hemoglobin<br />

molecule must be fully functional right<br />

from the start.<br />

b) In the embryonic stage (up to 3 months gestation)<br />

the oxygen transport needs are radically<br />

different. What has the Creator done to cater for<br />

this situation? He has specified the amino acid<br />

sequences in two of the protein chains in the<br />

hemoglobin molecules such that the spatial configuration<br />

after folding results in exactly the oxygen<br />

affinity required. Compared to HbA, instead<br />

of the two β chains there are two ε chains.<br />

Embryonic hemoglobin is thus also called Hbα 2 ε 2<br />

c) In the fetal stage (from 3 months gestation to<br />

birth), the oxygen requirements are different<br />

again. Now the two ε chains of the embryonic<br />

hemoglobin (Hbα 2 ε 2 ) are replaced by two γ<br />

chains. It is now called Hbα 2 ε 2 or HbF (= fetal).<br />

Throughout its development, the fetus must<br />

remain richly supplied with oxygen. Exchanges<br />

of respiratory gases and energy-laden substances<br />

take place in the placenta. If the fetus had the<br />

normal adult hemoglobin HbA, the blood would<br />

be only 60% saturated. Thus the Creator has for<br />

this stage provided the HbF, which is precisely<br />

tuned to the coupling of the fetal and maternal<br />

circulation. Because of its special 3-D structure,<br />

HbF can take up 20-30% more oxygen from the<br />

mother’s blood than HbA. The later replacement<br />

of HbF by HbA occurs through a remarkable<br />

process. Already prior to birth, a “switch of programming”<br />

takes place such that at birth the erythrocytes<br />

only contain some 60-80% of fetal<br />

hemoglobin. At three months of age, the HbF<br />

hemoglobin has been almost completely replaced<br />

by the HbA hemoglobin. It is amazing how all<br />

these processes take place in a completely goaldirected<br />

fashion, in response to the changing circumstances<br />

and needs.<br />

If one were to try to explain the origin of hemoglobin,<br />

and the complex machinery for its synthesis,<br />

from an evolutionary standpoint, there<br />

would be some massively insoluble problems:<br />

●<br />

How is it, that in all the three stages of<br />

human development described above, the<br />

exact chemical makeup (the sequences and

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