Hemoglobin compounds

Figure 15.2 Absorption spectra of hemoglobin compounds at the visible and near-infrared wavelengths. (From [4] copyright 1994 IEEE, with permission.)... 

An extensive experimental and theoretical investigation of the Mossbauer effect in hemoglobin compounds has recently been reported by G. Lang and W. Marshall Proc. Phys. Soc. 87, 3 (1966). 

Coryell was able to show that interactions occur in this system of hemoglobin compounds, both of which contain ionically bound iron, and that the interaction energy effect of approximately 2600 cal. per mole is involved. ... 

The wavelengths and millimolar extinction coefficients at the absorption peaks of several important hemoglobin compounds have been summarized by Lemberg and Legge (1949). A partial list of their values is given in Table I. 

It is proposed to polymerize the vinyl group of the hemin molecule with other vinyl comonomers to prepare model compounds to be used in hemoglobin research. Considering hemin and styrene to be species 1 and 2, respectively, use the resonance concept to rank the reactivity ratios rj and X2. 

The abihty of iron to exist in two stable oxidation states, ie, the ferrous, Fe ", and ferric, Fe ", states in aqueous solutions, is important to the role of iron as a biocatalyst (79) (see Iron compounds). Although the cytochromes of the electron-transport chain contain porphyrins like hemoglobin and myoglobin, the iron ions therein are involved in oxidation—reduction reactions (78). Catalase is a tetramer containing four atoms of iron peroxidase is a monomer having one atom of iron. The iron in these enzymes also undergoes oxidation and reduction (80). 

Synthetic Heme. Synthetic compounds that biad or chelate O2 have been produced. These compounds are commercially attractive because manufacture and Hcensure might be developed as a dmg, rather than as a biological product. It has been shown that synthetic hemes can be used to transfuse animals (53). Although synthetic O2 carriers would avoid the limited hemoglobin supply problem, the synthetic procedures are very tedious, and the possibihty of scale up seems remote. 

Pyridoxal Derivatives. Various aldehydes of pyridoxal (Table 3) react with hemoglobin at sites that can be somewhat controlled by the state of oxygenation (36,59). It is thereby possible to achieve derivatives having a wide range of functional properties. The reaction, shown for PLP in Figure 3, involves first the formation of a Schiff s base between the amino groups of hemoglobin and the aldehyde(s) of the pyridoxal compound, followed by reduction of the Schiff s base with sodium borohydride, to yield a covalendy-linked pyridoxyl derivative in the form of a secondary amine. 

PSS-SG composite film was tested for sorption of heme proteins hemoglobin (Hb) and myoglobin (Mb). The peroxidaze activity of adsorbed proteins were studied and evaluated by optical and voltammetric methods. Mb-PSS-SG film on PG electrode was shown to be perspective for detection of dissolved oxygen and hydrogen peroxide by voltammetry with linear calibration in the range 2-30 p.M, and detection limit -1.5 p.M. Obtained composite films can be modified by different types of biological active compounds which is important for the development of sensitive elements of biosensors. 

Kohlenozyd, n, carbon monoxide, -eisen, n. iron carbonyl, -gas, n. carbon monoxide gas. -hamoglobin, n. compound of carbon monoxide with hemoglobin, -kalium, n. potassium carboxide, potassium hexacar-bonyl. -knallgas, n, explosive mixture of carbon monoxide and oxygen, -nickel, n. nickel carbonyl. 

Of the ten trace elements known to be essential to human nutrition, seven are transition metals. For the most part, transition metals in biochemical compounds are present as complex ions, chelated by organic ligands. You will recall (Chapter 15) that hemoglobin has such a structure with Fe2+ as the central ion of the complex. The Co3+ ion... 

This series in heterocychc chemistry is being introduced to collectively make available critically and comprehensively reviewed hterature scattered in various journals as papers and review articles. All sorts of heterocyclic compounds originating from synthesis, natural products, marine products, insects, etc. will be covered. Several heterocyclic compounds play a significant role in maintaining life. Blood constituents hemoglobin and purines, as well as pyrimidines, are constituents of nucleic acid (DNA and RNA). Several amino acids, carbohydrates, vitamins, alkaloids, antibiotics, etc. are also heterocyclic compounds that are essential for life. Heterocyclic compounds are widely used in clinical practice as drugs, but all applications of heterocyclic medicines can not be discussed in detail. In addition to such applications, heterocyclic compounds also find several applications in the plastics industry, in photography as sensitizers and developers, and the in dye industry as dyes, etc. 

The 3D structure of the 2,3-diphosphoglycerate (DPG) complex of hemoglobin (Hb) served to derive simple aromatic dialdehydes that mimic the function of DPG as an allosteric modulator of the oxygen affinity of Hb. Some of the resulting compounds were as active and even more active than DPG, the natural ligand [1-3]. 

Hemoproteins, such as hemoglobin and the cytochromes, contain heme. Heme is an iron-porphyrin compound (Fe -protoporphyrin IX) in... 

Diphosphoglycerate A compound in red blood cells that affects oxygen binding to and release from hemoglobin. 

Hematological effects were noted in several animal studies. A few instances of significant differences were noted in the hematocytology (red blood cell [RBC] count, packed cell volume, hemoglobin, leukocyte count, and differential leukocyte count) in rats that had received diisopropyl methylphosphonate in the diet at doses of 0, 30, 100, or 300 mg/kg/day for 90 days. However, because the differences were so scattered and lacked clear dose response, they were considered of no toxicological importance (Hart 1976). Beagles that had been treated with the compound in the diet at doses of 4, 13, or 38 mg/kg/day for 14 days demonstrated values that were within normal limits for... 

The structures of the oxime complex Co(NO)(dmg)2 (84) and its diphenylglyoxime analog exhibit strongly bent Co—NO groups, which are easily oxidized to the corresponding nitro compound.353 A mechanistic study of NO transfer from Co(NO)(dmg)2 to hemoglobin established that the reaction involves NO association with the protein subsequent to dissociation of NO from the Co complex.354 This mechanism is also consistent with the observation of nitrato complexes in reactions... 

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