Metalloproteins proteins

Metalloprotein protein that binds a specific metal ion and requires that metal ion for proper function Metal transporter transmembrane protein responsible for the translocation of metal ions across a lipid bilayer MTMl mitochondrial inner membrane transporter needed for activating SOD2 with manganese SCO Copper carrying molecule, possibly the copper chaperone or copper insertion factor for cytochrome oxidase SMF2 intracellular metal transporter essential for manganese trafficking... 

For the construction of artificial metalloproteins, protein scaffolds should be stable, both over a wide range of pH and organic solvents, and at high temperature. In addition, crystal structures of protein scaffolds are crucial for their rational design. The proteins reported so far for the conjugation of metal complexes are listed in Fig. 1. Lysozyme (Ly) is a small enzyme that catalyzes hydrolysis of polysaccharides and is well known as a protein easily crystallized (Fig. la). Thus, lysozyme has been used as a model protein for studying interactions between metal compounds and proteins [13,14,42,43]. For example, [Ru(p-cymene)] L [Mn(CO)3l, and cisplatin are regiospecificaUy coordinated to the N = atom of His 15 in hen egg white lysozyme [14, 42, 43]. Serum albumin (SA) is one of the most abundant blood proteins, and exhibits an ability to accommodate a variety of hydrophobic compounds such as fatty acids, bilirubin, and hemin (Fig. lb). Thus, SA has been used to bind several metal complexes such as Rh(acac)(CO)2, Fe- and Mn-corroles, and Cu-phthalocyanine and the composites applied to asymmetric catalytic reactions [20, 28-30]. 

Metalloproteins, proteins with bound metal ions. To this family of transport and storage proteins belong, e.g., ferritin, transferrin, iron-sulfur proteins, metallothioneins [D. P. Ballou, Metalloproteins, Princeton University Press, 1999 A. Messerschmidt et al. (Eds.), Handbook of Metalloproteins, Vols. 1-4, John Wiley Sons, 2001-2004]. 

Computer simulations of electron transfer proteins often entail a variety of calculation techniques electronic structure calculations, molecular mechanics, and electrostatic calculations. In this section, general considerations for calculations of metalloproteins are outlined in subsequent sections, details for studying specific redox properties are given. Quantum chemistry electronic structure calculations of the redox site are important in the calculation of the energetics of the redox site and in obtaining parameters and are discussed in Sections III.A and III.B. Both molecular mechanics and electrostatic calculations of the protein are important in understanding the outer shell energetics and are discussed in Section III.C, with a focus on molecular mechanics. 

HEMOPROTEINS. These proteins are actually a subclass of metalloproteins because their prosthetic group is heme, the name given to iron protoporphyrin IX (Figure 5.15). Because heme-containing proteins enjoy so many prominent biological functions, they are considered a class by themselves. 

Fritz G, Heizmann CW (2004) 3D-structures of the Ca2+-and Zn2+-binding SI00 proteins. In Messerschmidt A, Bode W, Cygler M, Handbook of metalloproteins. Wiley, Chichester, pp, 529—540... 

Redox reactions of sulphur-containing amino-acid residues in proteins and metalloproteins. 

Weser U (1985) Redox Reactions of Sulphur-Containing Amino-Acid Residues in Proteins and Metalloproteins, an XPS Study. 61 145-160 Weser U (1973) Structural Aspects and Biochemical Function of Erythrocuprein. 17 1-65 Weser U, see Abolmaali B (1998) 91 91-190... 

The many redox reactions that take place within a cell make use of metalloproteins with a wide range of electron transfer potentials. To name just a few of their functions, these proteins play key roles in respiration, photosynthesis, and nitrogen fixation. Some of them simply shuttle electrons to or from enzymes that require electron transfer as part of their catalytic activity. In many other cases, a complex enzyme may incorporate its own electron transfer centers. There are three general categories of transition metal redox centers cytochromes, blue copper proteins, and iron-sulfur proteins. 

Injury to cells and tissues may enhance the toxicity of the active oxygen species by releasing intracellular transition metal ions (such as iron) into the surrounding tissue from storage sites, decompartmentalized haem proteins, or metalloproteins by interaction with delocalized proteases or oxidants. Such delocalized iron and haem proteins have the capacity to decompose peroxide to peroxyl and alkoxyl radicals, exacerbating the initial lesion. 

Table 9 gives some cases where the rotational strengths of absorption bands have been measured in metalloproteins. At the present time these changes are not used to diagnose the nature of the ligands of the metal but rather they have been used to follow minor changes at the metal when substrates or inhibitors interact with the metals. The sensitivity of CD and MCD measurements to very small changes in the metal environment make them very attractive for protein/metal complex studies. 

If we now look away from metalloproteins there are some obvious further connections between prokaryotes and eukaryotes but there are also other novelties such as the arrival of the proteins actin, myosin and tubulin associated with MgATP and mechanical activities. How did they arise ... 

Classes of metalloproteins. Transition ion prosthetic groups in proteins are... 

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