Transition metal complexes, cytochrome

In the following sections the effect of pressure on different types of electron-transfer processes is discussed systematically. Some of our work in this area was reviewed as part of a special symposium devoted to the complementarity of various experimental techniques in the study of electron-transfer reactions (124). Swaddle and Tregloan recently reviewed electrode reactions of metal complexes in solution at high pressure (125). The main emphasis in this section is on some of the most recent work that we have been involved in, dealing with long-distance electron-transfer processes involving cytochrome c. However, by way of introduction, a short discussion on the effect of pressure on self-exchange (symmetrical) and nonsymmetrical electron-transfer reactions between transition metal complexes that have been reported in the literature, is presented. 

McLain, J. L. Lee, J. Groves, J. T. Biomimetic oxygenations related to cytochrome P450 metal- and metal-peroxo intermediates, Biomimetic Oxidations Catalyzed by Transition Metal Complexes , Ed. Meunier, B. Imperial College Press London, 2000, pp. 91-169. 

In the last decade, transition metal complexes (e.g. metalloporphyrins) have been used to catalyze epoxidation. These entities can reproduce and mimic all reactions catalyzed by heme-enzymes (cytochromes P-450)54. Synthetic metalloporphyrins are analogous to the prosthetic group of heme-containing enzymes which selectively catalyze various oxidation reactions. The metallo complexes of Fe, Co, Cr, Mn, Al, Zn, Ru, etc. possessing porphyrin ligands have been mostly studied55 -57. Porphyrin ligands (4) are planar and can possess several redox states of the central metallic ions and hence they can exist as oxo metals. 

Transition metal complexes with heterocyclic ligands as models of flavaenzyme and cytochrome P450 92PAC403. 

Cytochrome c, a small heme protein (mol wt 12,400) is an important member of the mitochondrial respiratory chain. In this chain it assists in the transport of electrons from organic substrates to oxygen. In the course of this electron transport the iron atom of the cytochrome is alternately oxidized and reduced. Oxidation-reduction reactions are thus intimately related to the function of cytochrome c, and its electron transfer reactions have therefore been extensively studied. The reagents used to probe its redox activity range from hydrated electrons (I, 2, 3) and hydrogen atoms (4) to the complicated oxidase (5, 6, 7, 8) and reductase (9, 10, 11) systems. This chapter is concerned with the reactions of cytochrome c with transition metal complexes and metalloproteins and with the electron transfer mechanisms implicated by these studies. 

The ability to exist in more than one oxidation state allows transition-metal complexes to serve as the active site of enzymes whose function is to transfer electrons (39). A great deal of effort has been directed at understanding the mechanisms of electron transfer in metalloproteins, such as cytochromes and blue copper proteins (40). Of particular interest is the mechanism by which an electron can tunnel from a metal center that is imbedded in a protein matrix to a site on the outer surface of the protein (7). A discussion of current theories is given in this volume. 

Transition metal complexes of phthalocyanine encaged in faujasite type zeolites have been reported as efficient catalysts in the oxidation of alkanes at room temperature and atmospheric pressure [6-13]. These catalysts constitute potential inorganic mimics of remarkable enzymes such as monooxygenase cytochrome P-450 which displays the ultimate in substrate selectivity. In these enzymes the active site is the metal ion and the protein orientates the incoming substrate relative to the active metal center. Zeolites can be used as host lattices of metal complexes [14, 15]. The cavities of the aluminosilicate framework can replace the protein terciary structure of natural enzymes, thus sieving and orientating the substrate in its approach to the active site. Such catalysts are constructed by the so-called ship in a bottle synthesis the metal phthalocyanine complexes are synthesized in situ within the supercages of the zeolite... 

The metalloproteins consist of a metal complex imbedded in and bonded to a protein net of covalently bonded amino acids. The most commonly studied systems are the myoglobins and cytochromes, which contain Fe(II) or Fe(III) in a porphyrin complex, or the copper blue proteins, which have Cu(II) or Cu(I) compiexed most often by histidine nitrogens and cysteine and methionine sulfurs from the protein. Metalloproteins can be oxidized or reduced by standard transition-metal complex reagents, and the latter usually are chosen to ensure outer-sphere electron transfer. This area has been the subject of numerous reviews. 

Analysis of d-d spectra of transition-metal complexes can give information about three parameters of structural importance the symmetry of the species, the magnitude of A, and the magnitude of the Racah parameter B. Identifying the symmetry and coordination number of a complex is obviously important in determining its stmcture. Xhe number of methods available for studying complicated species in solution is limited, and electronic spectroscopy is useful in this context. Xhe electronic spectmm of nickel cytochrome c, for example, is interpreted as showing that the nickel atom is six-coordinated, rather than four-coordinated. A... 

Breslow R, GeUman SH. Intramolecular nitrene C-H insertion mediated by transition-metal complexes as nitrogen analogues of cytochrome P-450 reactions. J Am Chem Soc. 

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