Hemocyanins model systems

Oxygenation rates were first examined for the system [Cu (R-XYL-H)]2+. In the model described here, two bis [2-(2-pyridyl)ethyl] amine (PY2) units are linked by a xylyl spacer group (R = H). Although initially proposed as a crude hemocyanin model, this system now is studied as a model for tyrosinase and is an example of hydrocarbon oxygenation taking place under mild conditions—that is, < 1 atm 02... 

This discussion of copper-containing enzymes has focused on structure and function information for Type I blue copper proteins azurin and plastocyanin, Type III hemocyanin, and Type II superoxide dismutase s structure and mechanism of activity. Information on spectral properties for some metalloproteins and their model compounds has been included in Tables 5.2, 5.3, and 5.7. One model system for Type I copper proteins39 and one for Type II centers40 have been discussed. Many others can be found in the literature. A more complete discussion, including mechanistic detail, about hemocyanin and tyrosinase model systems has been included. Models for the blue copper oxidases laccase and ascorbate oxidases have not been discussed. Students are referred to the references listed in the reference section for discussion of some other model systems. Many more are to be found in literature searches.50... 

Activation mechanism. What happens during activation in hemocyanins and how can we use them as model systems to understand tyrosinase/catecholoxidase activity Arthropod and mollusc hemocyanins have to be considered separately, although the processes are similar. 

Enzymes and proteins containing binuclear copper centers for the utilization of oxygen in organisms have attracted a great deal of attention in recent years. These proteins play critical roles in transport (hemocyanin), neurotransmitter synthesis (dopamine-P-hydroxylase),2 and pigment synthesis (tyrosinase), among other functions. Studies on natural systems as well as on model systems have led to further insight into the processes... 

For keyhole limpet hemocyanine (KLH) both antibody responses and delayed type hypersensitivity (DTH) reactions can be determined [43—45]. In addition several infectious models, including bacterial, viral and parasitic infections may be used to challenge the immune system [18,46]. As survival and eradication of the infections is the primary function of the immune system, these models provide direct information on the functional status of the immune system. Direct immunotoxic compounds will induce immunosuppression and thus an increase in infection rate and/or severity of the infection. The number of infectious agents (bacteria, parasites, or viral colonyforming units), increased morbidity and mortality are indications for an immunotoxic effect. Also a reduction in specific antibody levels in animals treated with the test compound compared to nontreated controls indicates immunosuppression. 

Like hemerythrin, hemocyanin is an oxygen transport non-heme-containing protein found in some arthropods and molluscs (104,105). In the 02-bound form, hemocyanin contains an antiferromagnetically coupled binuclear copper(II) system (106) ligated by histidine residues, with a sideways / 2-v2 V2 peroxo group bound to both Cu11 centers (104), which superseded the previous model (107). 

Optical absorption and CD spectrum of oxy-Hemocyanin and the model complex While the spectrum of oxy-Hc is typical for ii-rf. f Cu peroxo systems with an almost... 

Formation of metal-oxo species first became realistic in model studies on heme oxygenases (shunt path), and it has also become popular in nonheme systems. As for the metal-jd-peroxo species, the distinctive example of model study has appeared in the copper enzymes. The type 7 peroxo species has been proposed first based on models for dicopper oxy-hemocyanin [19, 20] before demonstration of the same oxygen bonding in enzyme [13]. The type 7 x-peroxo structure has been applied to diiron species in sMMO [14] in addition to 6 [21]. (see Chapter 8)... 

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