Cytochrome zinc

A trianionic zinc porphyrin anchored to a membrane by an imidazole link has been used to bind cytochrome c at the membrane surface. UV spectra confirmed the insertion of the zinc porphyrin into the phospholipid vesicle and was used to study surface association of cytochrome c. 

Zinc is also used in biological studies to gain information about non-zinc containing systems. It can be a convenient redox inactive replacement for the study of complex systems with multiple redox centers. For example, the mechanism of quenching the triplet state of zinc cytochrome c by iron(II) and iron(III) cytochrome c has been studied. Zinc insertion has been used to get around the difficulty of studying two heme proteins with the same absorption spectra and provides rate constants for iron and iron-free cytochrome c quenching.991... 

C. Shen and N.M. Kostic. Kinetics of photoinduced electron-transfer reactions within sol-gel silica glass doped with zinc cytochrome c. Study of electrostatic effects in confined liquids. J. Am. Chem. Soc. 119, 1304-1312 (1997). 

As a rule, oxygen radical overproduction in mitochondria is accompanied by peroxidation of mitochondrial lipids, glutathione depletion, and an increase in other parameters of oxidative stress. Thus, the enhancement of superoxide production in bovine heart submitochondrial particles by antimycin resulted in a decrease in the activity of cytochrome c oxidase through the peroxidation of cardiolipin [45]. Iron overload also induced lipid peroxidation and a decrease in mitochondrial membrane potential in rat liver mitochondria [46]. Sensi et al. [47] demonstrated that zinc influx induced mitochondrial superoxide production in postsynaptic neurons. 

Copper is part of several essential enzymes including tyrosinase (melanin production), dopamine beta-hydroxylase (catecholamine production), copper-zinc superoxide dismutase (free radical detoxification), and cytochrome oxidase and ceruloplasmin (iron conversion) (Aaseth and Norseth 1986). All terrestrial animals contain copper as a constituent of cytochrome c oxidase, monophenol oxidase, plasma monoamine oxidase, and copper protein complexes (Schroeder et al. 1966). Excess copper causes a variety of toxic effects, including altered permeability of cellular membranes. The primary target for free cupric ions in the cellular membranes are thiol groups that reduce cupric (Cu+2) to cuprous (Cu+1) upon simultaneous oxidation to disulfides in the membrane. Cuprous ions are reoxidized to Cu+2 in the presence of molecular oxygen molecular oxygen is thereby converted to the toxic superoxide radical O2, which induces lipoperoxidation (Aaseth and Norseth 1986). 

H. Koloczek, T. Horie, T. Yonetani, H. Anni, G. Maniara, and J. M. Vanderkooi, Interaction between cytochrome c and cytochrome c peroxidase Excited-state reactions of zinc- and tin-substituted derivatives, Biochemistry 26, 3142-3148 (1987). 

The standard formalisms for describing ET processes assume that in reactions such as Eqs. (1) and (2) there is but a single stable conformational form for each of the precursor and successor electron-transfer states. However, for a system that displays two (or more) alternative stable conformations with different ET rates, dynamic conformational equilibrium can modulate the ET rates. Major protein conformational changes can occur at rates that are competitive with observed rates of ET [9], and such gating [10] may occur in non-rigid complexes such as that between zinc cytochrome c peroxidase (ZnCcP) and cytochrome c (see below) or even within cytochrome c [5]. 

Substitution of zinc(ll) ions into cytochrome c peroxidase (ZnCcP) has been used to exploit photoactivation of electron transfer (eT) reactions since the mid-1990s. The ZnCcP triplet state ( ZnCcP) reduces Fe(III) cytochrome c, and then back electron transfer recombines the charge separation to complete the catalytic cycle (see Figure 7.36). 

In the experiment, ZnCcP is produced by laser photolysis, then transient absorption spectroscopy follows the formation (k ) and decay (/Ceb) of ZnCcP + in wild-type and mutant crystals. Kang and Crane have studied the effects of interface mutations on electron transfer rates in single crystals using complexes between a zinc-substituted cytochrome c peroxidase (ZnCcP) and site-directed mutants of yeast cytochrome c (yCc).The mutants replaced the... 

Transition metal hydroperoxo species are well established as important intermediates in the oxidation of hydrocarbons (8,70,71). As they relate to the active oxygenating reagent in cytochrome P-450 monooxygenase, (porphyrin)M-OOR complexes have come under recent scmtiny because of their importance in the process of (poiphyrin)M=0 formation via 0-0 cleavage processes (72-74). In copper biochemistry, a hydroperoxo copper species has been hypothesized as an important intermediate in the catalytic reaction of the copper monooxygenase, dopamine P-hydroxylase (75,76). A Cu-OOH moiety has also been proposed to be involved in the disproportionation of superoxide mediated by the copper-zinc superoxide dismutase (77-78). Thus, model Cun-OOR complexes may be of... 

The last column in the table lists some of the functions of minerals. It should be noted that almost all of the macroelements in the body function either as nutrients or electrolytes. Iodine (as a result of its incorporation into iodothyronines) and calcium act as signaling substances. Most trace elements are cofactors for proteins, especially for enzymes. Particularly important in quantitative terms are the iron proteins hemoglobin, myoglobin, and the cytochromes (see p. 286), as well as more than 300 different zinc proteins. 

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