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Heme proteins reactions

Fig. 1 Reactions involving molecular oxygen and its reduced congeners in heme proteins. Reactions where equilibria are manifest are indicated as such. In globins, peroxidases, cytochrome oxidases, and heme oxygenases, the axial ligand X is a protein-derived histidine in catalases, X is a tyrosine phenolate in chloroperoxidases and cytochromes P450, X is a cysteine thiolate... Fig. 1 Reactions involving molecular oxygen and its reduced congeners in heme proteins. Reactions where equilibria are manifest are indicated as such. In globins, peroxidases, cytochrome oxidases, and heme oxygenases, the axial ligand X is a protein-derived histidine in catalases, X is a tyrosine phenolate in chloroperoxidases and cytochromes P450, X is a cysteine thiolate...
Zhu L, Sage J T and Champion P M 1994 Observation of coherent reaction dynamics in heme proteins Science 266 629-32... [Pg.1998]

Isocyanides [RNC] (174, 175) are isoelectronic with CO and have been extensively used as CO analogs in studies of heme proteins (176-180). W-Butyl isocyanide (N-BIC) behaves as a CO analog at both the CODH and ACS active sites (181). N-BIC competes with CO in the CO oxidation reaction, is a sluggish reductant, and causes EPR spectral changes at Clusters A, B, and C similar to those elicited by CO. [Pg.320]

The current example illustrates PVDOS formulation as an effective basis for comparison of experimental and theoretical NIS data for ferrous nitrosyl tetraphe-nylporph3Tin Fe(TPP)(NO), which was done [101] along with other ferrous nitrosyl porphyrins. Such compounds are designed to model heme protein active sites. In particular, the elucidation of the vibrational dynamics of the Fe atom provides a unique opportunity to specifically probe the contribution of Fe to the reaction dynamics. The geometrical structure of Fe(TPP)(NO) is shown in Fig. 5.16. [Pg.193]

Ligand substitution reactions of NO leading to metal-nitrosyl bond formation were first quantitatively studied for metalloporphyrins, (M(Por)), and heme proteins a few decades ago (20), and have been the subject of a recent review (20d). Despite the large volume of work, systematic mechanistic studies have been limited. As with the Rum(salen) complexes discussed above, photoexcitation of met allop or phyr in nitrosyls results in labilization of NO. In such studies, laser flash photolysis is used to labilize NO from a M(Por)(NO) precursor, and subsequent relaxation of the non-steady state system back to equilibrium (Eq. (9)) is monitored spectroscopically. [Pg.208]

The kinetics of reactions of NO with ferri- and ferro-heme proteins and models under ambient conditions have been studied by time-resolved spectroscopic techniques. Representative results are summarized in Table I (22-28). Equilibrium constants determined for the formation of nitrosyl complexes of met-myoglobin (metMb), ferri-cytochrome-c (Cyt111) and catalase (Cat) are in reasonable agreement when measured both by flash photolysis techniques (K= konlkQff) and by spectroscopic titration in aqueous media (22). Table I summarizes the several orders of magnitude range of kon and kQs values obtained for ferri- and ferro-heme proteins. Many k0f[ values were too small to determine by flash photolysis methods and were determined by other means. The small values of kQ result in very large equilibrium constants K for the... [Pg.210]

The low reactivity of both Cyt111 and Cyt11 toward NO can be attributed to occupation of the heme iron axial coordination sites by an imidazole nitrogen and by a methionine sulfur of the protein (28). Thus, unlike other heme proteins where one axial site is empty or occupied by H20, formation of the nitrosyl complex not only involves ligand displacement but also significant protein conformational changes which inhibit the reaction with NO. However, the protein does not always inhibit reactivity given that Cat and nNOS are more reactive toward NO than is the model complex Fem(TPPS)(H20)2 (Table II). Conversely, the koS values... [Pg.211]

In order for NO to act as an intracellular signaling agent at sub-micromolar concentrations, it must be generated near the target, and the reactions with ferro-hemes must be very fast to compete with other chemical and physiological processes leading to NO depletion. The above study is consistent with the intuitive notion that the fast reactions of ferro-heme proteins with NO are due to a vacant or exceedingly labile coordination site. [Pg.217]

Flash photolysis techniques were unsuitable for measuring the slow off reactions for the iron(II) model complexes such as Fen(TPPS)(NO), since the experimental uncertainties in the extrapolated intercepts of kohs vs. [NO] plots were larger than the values of the intercepts themselves. When trapping methods were used to evaluate NO labilization from FeII(TPPS)(NO), k(,n values were found to be quite small but were sensitive to the nature of the trapping agents used. Lewis bases that could coordinate the metal center appeared to accelerate NO loss. More reliable estimates for the uncatalyzed off reaction were obtained by using Ru(edta)- as an NO scavenger, and the koS values listed in Table I were obtained in this manner (21c). The small kQ values found for Fe(II) models are consistent with the trend observed for the ferro-heme proteins discussed above. [Pg.217]

Additional mechanistic insight into the reductive nitrosylation of ferri-heme proteins was obtained from kinetic studies carried out on aqueous solutions of Cytm, metMb, and metHb at various pH values (67). For example, Cytm undergoes reduction by NO to Cyt11 in aqueous solutions at pH values > 6.5. A hypothetical reaction mechanism is shown in Scheme 2 which would predict the rate law presented in Eq. (31) (67). [Pg.225]

Given that hydroxylamine reacts rapidly with heme proteins and other oxidants to produce NO [53], the hydrolysis of hydroxyurea to hydroxylamine also provides an alternative mechanism of NO formation from hydroxyurea, potentially compatible with the observed clinical increases in NO metabolites during hydroxyurea therapy. Incubation of hydroxyurea with human blood in the presence of urease results in the formation of HbNO [122]. This reaction also produces metHb and the NO metabolites nitrite and nitrate and time course studies show that the HbNO forms quickly and reaches a peak after 15 min [122]. Consistent with earlier reports, the incubation ofhy-droxyurea (10 mM) and blood in the absence of urease or with heat-denatured urease fails to produce HbNO over 2 h and suggests that HbNO formation occurs through the reactions of hemoglobin and hydroxylamine, formed by the urease-mediated hydrolysis of hydroxyurea [122]. Significantly, these results confirm that the kinetics of HbNO formation from the direct reactions of hydroxyurea with any blood component occur too slowly to account for the observed in vivo increase in HbNO and focus future work on the hydrolytic metabolism of hydroxyurea. [Pg.193]

Reaction of nitric oxide with ferrohemoproteins produces paramagnetic NO-ligated heme proteins (S = 1/2, rhombic g tensors with principal values in the range 1.96-2.08). In many compounds studied so far by EPR the hf interaction of the NO nitrogen and of a second axial nitrogen is clearly resolved in the intermediate g-value region near... [Pg.94]

There is currently much interest in electron transfer processes in metal complexes and biological material (1-16, 35). Experimental data for electron transfer rates over long distances in proteins are scarce, however, and the semi-metheme-rythrin disproportionation system appears to be a rare authentic example of slow electron transfer over distances of about 2.8 nm. Iron site and conformational changes may also attend this process and the tunneling distances from iron-coordinated histidine edges to similar positions in the adjacent irons may be reduced from the 3.0 nm value. The first-order rate constant is some 5-8 orders of magnitude smaller than those for electron transfer involving some heme proteins for which reaction distances of 1.5-2.0 nm appear established (35). [Pg.222]

In protein-protein reactions, the donor-acceptor distance is determined by the structure of the reacting proteins, and the way(s) in which they bind and interact. For example, it is generally believed that cytochrome c binds to its reaction partners at or near the exposed heme edge, in order to minimize the reactant distance and thereby maximize the rate. The redox active centers of most proteins are sufficiently buried that the large protein imposed distances provide low intrinsic reactivity for the proteins with respect to exogenous... [Pg.160]

The study of the dynamics of spin-state changes is important for the understanding of the kinetics of bimolecular electron transfer reactions ° and racemization and isomerization processes (Sec. 7.5.1). Low spin — high spin equilibria, often attended by changes in coordination numbers, are observed in some porphyrins and heme proteins, although their biological significance is, as yet, uncertain. [Pg.339]

In the presence of ascorbate and oxygen, oxyMb and other heme proteins undergo a series of reactions that resemble the catalytic cycle of HO, albeit with less efficiency 278-281). Although the spectroscopic similarities of Mb and corresponding derivatives of HO are remarkable 264, 267, 272), the mechanism of the coupled oxidation reaction... [Pg.35]

The biphasic reaction with CO points to the existence of multiple heme-hemopexin conformers, and this is borne out by spectral analyses. The absorbance spectra of rabbit ferri-, ferro-, and CO-ferro-mesoheme-hemopexin are entirely analogous to those of other bis-histidyl heme proteins such as cytochrome 65 142), but the CD spectra exhibit unusual features (Fig. 11). Of particular interest are the weak signal of the ferro complex and the bisignate signal of the CO-ferro complex (also seen in the NO-ferro-mesoheme-hemopexin complex (140) and in human ferri-protoheme—hemopexin (139)). [Pg.224]


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See also in sourсe #XX -- [ Pg.452 , Pg.453 , Pg.454 ]




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