Metal proteins

Strohmeier W (1968) Problem und Modell der homogenen Katalyse. 5 96-117 Sugiura Y, Nomoto K (1984) Phytosiderophores - Structures and Properties of Mugineic Acids and Their Metal Complexes. 58 107-135 Sun H, Cox MC, Li H, Sadler PJ (1997) Rationalisation of Binding to Transferrin Prediction of Metal-Protein Stability Constants. 88 71-102 Swann JC, see Bray RC (1972) II 107-144... 

As examples. Table 8 records some observations on d—d and charge transfer absorption bands in metal/protein systems. The examination of the spectrum of cobalt carbonic anhydrase (d—d) and of iron conalbumin (charge-transfer) permitted a prediction of the ligands from the protein to the metal. The predictions have now been substantiated by other methods. 

Up until the time of publication of reference 38, there had been few modeling studies of metal-amino acid, metal-protein, metal-nucleotide, or metal-nucleic... 

Harrison, P. M., ed., Metalloproteins Part 1 Metal Proteins with Redox Roles, Verlag Chemie GmbH, Weinheim, 1985. 

Some pyridine-containing ligands of this type have been used to mimic the protein environment in non-heme iron metal proteins. The ligands L (10 and 11) tend to bind strongly to five positions of the coordination sphere leaving the sixth position available to bind unidentate ligands X [FeLX]w+. 

The chelate effect in proteins is also important, since the three-dimensional (3-D) structure of the protein can impose particular coordination geometry on the metal ion. This determines the ligands available for coordination, their stereochemistry and the local environment, through local hydrophobicity/hydrophilicity, hydrogen bonding by nearby residues with bound and non-bound residues in the metal ion s coordination sphere, etc. A good example is illustrated by the Zn2+-binding site of Cu/Zn superoxide dismutase, which has an affinity for Zn2+, such that the non-metallated protein can extract Zn2+ from solution into the site and can displace Cu2+ from the Zn2+ site when the di-Cu2+ protein is treated with excess Zn2+. 

A few years later, in 1953, the versatility of pyridoxal phosphate was illustrated by Snell and his collaborators who found many of the enzyme reactions in which pyridoxal phosphate is a coenzyme could be catalyzed non-enzymically if the substrates were gently heated with pyridoxal phosphate (or free pydridoxal) in the presence of di- or tri-valent metal ions, including Cu2+, Fe3+, and Al3+. Most transaminases however are not metal proteins and a rather different complex is formed in the presence of the apoprotein. 

Ritchie, C.W., Bush, A.I., Masters, C.L. (2004) Metal-protein attenuating compounds and Alzheimer s disease. Expert Opin. Investig. Drugs, 13, 1585-1592. 

Protein-Conformation Effects on the Metal-Protein Linkage. Since we have been unable to find model Ni-porphyrin complexes whose Raman frequencies come close to those of the Ni-reconstituted proteins, it is clear that the protein matrix has an impressive effect on axial ligation. We might also ask what is the effect of changes in protein conformation on axial ligation. 

Scheme 2.19 Asymmetric reduction of alkene 46 using a hybrid transition metal/protein catalyst.

Breslow, E. (1973). Metal—protein complexes. In Inorganic Biochemistry (G. L. Eichhorn, ed.), pp. 227-249. Elsevier, Amsterdam. 

Freeman, H. C., and Golomb, M. L. (1970). Model compounds for metal-protein interaction Crystal structure of three platinum(Il) complexes of l- and DL-methionine and glycyl-L-methionine. Chem. Commun. pp. 1523-1524. 

This volume of Advances in Protein Chemistry is the first in which all articles address a single specialized theme within protein science—metal-protein interactions from a structural perspective. Future volumes of Advances in Protein Chemistry will include other thematic volumes in which the reviews will cover different aspects of a single broad area and, as in the past, collections of reviews on a variety of major topics. 

The first article in this volume, by Jenny P. dusker, treats general aspects of metal liganding to functional groups in proteins. This article presents a detailed summary of the geometry of interaction of metals with the various chemical groups of proteins. It also presents, in Sections I through VIII, a lucid development of the principles and terminology of the field of metal-protein interactions. It is with these sections that the newcomer to the field of metalloproteins should start. 

Degradation of Tetracyclines Tetracyclines are relatively stable under acidic conditions but not under alkaline conditions. They form complexes with chelating agents such as divalent metals, proteins, and silanol groups (Oka et al., 2000 ... 

A useful concept for the classification of metal-containing proteins has been suggested by Vallee The proteins are divided into two groups metalloproteins and metal-protein complexes, on the basis of their stability during the isolation procedures. Metalloproteins retain their metal constituent during fractionation and there is a stoichiometric relationship between the metal and protein. On the other hand, the metal is loosely bound and easily lost during dialysis in metal-proteins. Examples of both types of proteins can be found in an article by Vallee and Coleman... 

The literature is rich with examples of metal-nitrosyl complexes, and it would be surprising if the generation of NO by the immune system did not result in the formation of many such adducts. Previous articles have presented summaries of metal proteins that form NO complexes (Butler et al., 1985 Henry et al., 1993), and more recently evidence has mounted that generation of NO by the immune system and by endothelial cells produces a variety of iron-nitrosyl complexes (Mulsch et al., 1993 Vanin et al., 1993 Lancaster et al., 1994). It is unclear which of the potential products will prove to be of physiological relevance, but because the enzymes that may be involved range from the central focus of oxidative cellular metabolism (LoBrutto et al., 1983) to the enzymes of DNA repair (Asahara et al., 1989), the list of potential targets is long and varied. 

There are many other proteins that resemble the scavenger metal proteins, but they scavenge for quite other chemical groups. All the histones are proteins with multiple repeating sequences of the kind... 

In these compounds the cobalt atom is enclosed in a highly conjugated cobalamin structure and linked to an alkyl group via a metal-carbon bond. The B12 coenzymes are diamagnetic and can be regarded as complexes of cobalt(III) with a carbanion as a ligand (2). As this review will be limited to cases of direct metal-protein interactions the corrinoids will not be discussed further. 

In the present section, analogies and similarities will be noted between enzymes and heterogeneous catalysts in the concept of the active site and metal-protein/metal-support analogies the possession of size and shape selectivity the similarity or identity in kinetics between the two processes the use of electrochemical organization on a molecular or supramolecular level the possibility of... 

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