Hemoglobin reaction with oxygen

Fig. 3. Diagrammatic sketch showing the change in tertiary structure of a hemoglobin a chain on reaction with oxygen. Movement of the iron atom into the plane of the porphyrin ring causes a movement of helix F toward helix H, which expels tyrosine in position 140 from its pocket between the two helices. From (PIO), M. F. Perutz, Stereochemistry of cooperative effects in haemoglobin. Nature (London) 228, 726 (1970) with permission of the author and publisher.

The synthesis and turnover of porphyrins that are precursors of heme are important hecanse of the central role of heme proteins, hemoglobin, and the cytochromes in reactions with oxygen and in electron transfer. Qnantitatively, hemoglobin synthesis is a major part of the nitrogen economy in hitmans. 

CAN YOU ANSWER THIS What would happen if fetal hemoglobin had the same equilibrium constant for the reaction with oxygen as adult hemoglobin ... 

Optimization of the ATP—hemoglobin reaction conditions produced a preparation having a markedly reduced oxygen affinity. Five fractions from a reaction mixture, when isolated, were found to have P q values ranging from 1.1 to 5.0 kPa (8 to 38 torr), most withUtfle cooperativity (118). These results are consistent with those found with other polyfunctional reagents that react on the surface of hemoglobin. 

Carbon monoxide seriously impedes transport of oxygen. The deadly effect of inhaled CO results from its reaction with hemoglobin. A CO molecule is almost the same size and shape as O2, so it fits into the binding pocket of the hemoglobin molecule. In addition, the carbon atom of CO forms a stronger bond to than does O2. Under... 

This entire reaction is reversed when the blood reaches the lungs. Because carbon dioxide is eliminated by ventilation, the reaction is pulled to the left. Bicarbonate ions diffuse back into the red blood cells. The hemoglobin releases the hydrogen ions and is now available to load up with oxygen. The bicarbonate ions combine with the hydrogen ions to form carbonic acid, which then dissociates into carbon dioxide and water. The carbon dioxide diffuses down its concentration gradient from the blood into the alveoli and is exhaled. A summary of the three mechanisms by which carbon dioxide is transported in the blood is illustrated in Figure 17.8. 

Selected entries from Methods in Enzymology [vol, page(s)] Activity in ethanol oxidation, 233, 118 in hydroxyethyl radical formation analysis with reconstituted vesicles, 233, 127 characterization, 233, 123-125 monooxygenase activity, 231, 574-575 reductase [hemoglobin-catalyzed reactions with, 231, 573-574 oxygen concentration and, 231, 579 pH dependence, 231, 580 reaction mixtures, 231, 578 oxygen content, measurement, 231, 587-588 reductase concentration and, 231, 580 time dependence, 231, 578 preparation, 231, 577]. 

F.B. Jensen, Nitric oxide formation from the reaction of nitrite with carp and rabit hemoglobin at intermediate oxygen saturations. FEBS J. 275, 3375-3387 (2008)... 

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