Oxygen-myoglobin reaction

NSPORT metal ion EXCHANGE TIMES MICROENVIRONMENT MULTIPLE ATTACK UCLEOPHILIC SUBST TUTION REACTION NONLINEAR INHIBITION RANDOM SCISSIOI VTE MFC MYOGLOBIN OXYGENATION NUCLEATION ONE DIMENSIONA... 

If the myoglobin-oxygen binding reaction occurs rapidly enough that it is maintained near equilibrium, then S° can be computed... 

It will be seen that values of Am for catalase and peroxidase are very similar, and not unlike the value of Ao for the oxygen reaction of myoglobin. The values of At// vary widely. It may be pointed out that Chance s results on peroxidase are of great interest not only in this connection but also as the most direct verification so far obtained of the Michaelis (22, 135) theory of the enzyme-substrate complex. 

B.C. King and F.M. Hawkridge, A study of the electron transfer and oxygen binding reactions of myoglobin. J. Electroanal. Chem. 237, 81-92 (1987). 

Compared with Molsidomine, both SIN-1 and SIN-1A are reported to induce similar, but more rapid hypotensive action [95, 96]. SIN-1A, after undergoing oxidation in the presence of oxygen or, in vivo, possibly by redox-active enzymes such as cytochrome C [97, 98] or by reaction with ferric myoglobin formed during reperfusion injury [99], releases NO through an intermediate radical cation. 

Protein functions and interactions are infinitely varied in biological species— one of the major problems associated with complete classification of any proteome. Proteins may transport substances myoglobin and hemoglobin (discussed in Chapter 7) transport oxygen, and carbon dioxide, in mammalian blood. Proteins called enzymes catalyze necessary biochemical reactions. The active site of an enzyme contains those amino acids that come in direct contact... 

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