Biological activity of hemoprotein nitrosyl complexes
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Hemeprotein
The aim of this paper was to measure the binding of CO to myoglobin and hemoglobin at various PO2 values. For this purpose we have studied an "in vitro" system made up of solutions of hemoglobin and myoglobin equilibrated in two connected tonometers with the same gas phase of various PO2 and PCO. The results indicate that a significant proportion of CO is released by hemoglobin and binds myoglobin at low PO2 values (approximately 2-3 Torr), in qualitative agreement with the predictions of a previous computer simulation of the "in vivo" system.
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Several methods were used to estimate quantitatively the myoglobin and hemoglobin concentration in beef muscle extracts. Of the methods used, determinations based on the conversion of these pigments in muscle extracts to carbon monoxide compounds provided the most favorable results. This method was tested with solution mixtures of myoglobin and hemoglobin of pre-determined concentrations. The total pigment concentration, as well as percentages of the two component pigments, were in close agreement with the values of the test solution mixtures.
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The two main heme proteins, hemoglobin and myoglobin, are important factors determining meat quality aspects such as color and hemorrhage. The extent of hemorrhage in muscle tissue can probably be determined by measuring the hemoglobin content. The objective of this study was twofold: 1) to develop a specific and reproducible method to quantify the hemoglobin and myoglobin content in muscle tissue of broiler chickens, and 2) to study the effect of hemorrhage on the hemoglobin content in muscle tissue. We tested several methods to determine the total heme, hemoglobin, and myoglobin content in broiler chicken muscles on their specificity, sensitivity, and reproducibility. Methods based on immunological techniques appeared to be very specific and sensitive. The results obtained applying these methods on muscle tissue extracts were, however, not reproducible due to concentration effects. A combination of spectrophotometric analysis of the total heme protein concentration and measurement of the myoglobin concentration, applying size exclusion chromatography, proved to be a reliable and reproducible method to determine the hemoglobin and myoglobin content in chicken muscles. The total heme, hemoglobin, and myoglobin contents were related to muscle type. Extensive hemorrhage increased the hemoglobin content.
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The effects of heme removal on the molecular structure of tuna and sperm whale myoglobin have been investigated by comparing the solvent accessibility to the heme pocket of the two proteins with that of the corresponding apoproteins. Although the heme microenvironment of tuna myoglobin is more polar than that of sperm whale myoglobin, the accessibility of solvent to heme is identical in the two proteins as revealed by thermal perturbation of Soret absorption. The removal of heme produces loss of helical folding and increase of solvent accessibility but the effects are rather different for the two proteins. More precisely, the loss of helical structure upon heme removal is 50% for tuna myoglobin and 15% for sperm whale myoglobin; moreover, the solvent accessibility of the heme pocket of tuna apomyoglobin is 2–3‐fold greater than that of sperm whale apomyoglobin. These results have been explained in terms of the lack of helical folding in segment D, the structural organization of which may have a relevant effect in regulating the accessibility of ligands to the heme. The effects produced by charged quenchers reveal that the ligand path from the surface of the molecule to the ion atom of the heme involves a positively charged residue which may reasonably be identified as Arg‐45 (sperm whale myoglobin) or Lys‐41 (tuna myoglobin) on the basis of recent X‐ray crystallographic information.
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Myoglobin, one of the hemoproteins, is a well-known protein which has a protoporphyrin IX iron complex via noncovalent interaction. Therefore, a myoglobin with a synthetic heme is readily available by reconstitutional method. We have recently prepared various heme moieties having modified heme-propionates and incorporated them into an apomyoglobin to obtain a reconstituted protein. The myoglobin has an artificially created interface which acts as the binding domain to form a protein-protein or protein-small substrate complex. As a result, the myoglobin is converted to an electron transfer protein or oxidase. Thus, the present method gives a unique function to the myoglobin surface. Furthermore, it is found that the modification of heme framework is also an attractive approach to improving physiological function of hemoproteins. For example, an iron porphycene as a structural isomer of the heme is a good prosthetic group for the myoglobin to show a high dioxygen affinity. The net results propose that the reconstitutional method of hemo-proteins will serve as a new way in creating a functionalized protein by organic synthetic method.
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For the quantitative determination of hemoglobin concentration in heart muscle it is important to distinguish between myoglobin and hemoglobin, two dyes with very similar optical absorption properties. With an isolated perfused pig heart model and EMPHO II SSK we measured tissue spectra in the visible range before and after adding erythrocytes to the perfusate. By calculating light intensity differences we were able to show spatial hemoglobin distribution in heart muscle.
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Myoglobin will be a good scaffold for engineering a function into proteins. To modulate the physiological function of myoglobin, almost all approaches have been demonstrated by site-directed mutagenesis, however, there are few studies which show a significant improvement in the function. In contrast, we focused on the replacement of heme in the protein with an artificial prosthetic group. Recently, we prepared a novel myoglobin reconstituted with an iron porphycene as a structural isomer of mesoheme. The bluish colored reconstituted myoglobin is relatively stable and the deoxymyoglobin reversibly binds ligands. Interestingly, the O2 affinity of the reconstituted myoglobin, 1.1 × 109 M-1, is a significant 1,400-fold higher than that of the native myoglobin. Furthermore, the unfavorable autoxidation kinetics show 7-fold decrease in rate for the reconstituted myoglobin relative to the native myoglobin, indicating the stable oxy-form against autoxidation. The net results come from the slow dissociation of the O2 ligand in the reconstituted myoglobin, koff = 0.11 s-1, because of the formation of strong hydrogen bond between His64 and negatively charged dioxygen. The present study indicates that the replacement of native heme with an artificially created prosthetic group will give us a unique function into a hemoprotein.
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