Iron in proteins

The Debye temperature is usually high for metallic systems and low for metal-organic complexes. For metals with simple cubic lattices, for which the model was developed, is found in the range from 300 K to well above 10 K. The other extreme may be found for iron in proteins, which may yield d as low as 100-200 K. Figure 2.5a demonstrates how sharply/(T) drops with temperature for such systems. Since the intensity of a Mossbauer spectrum is proportional to the... 

David (D9) determined iron in plants and gives detailed instructions for the treatment of plant samples, entailing acid digestion and filtration before aspiration. The determination of iron in protein solutions is briefly mentioned (M2a). 

Becker, J. S., Zoriy, M., Krause-Buchholz, U., Becker, J. S., Pickhardt, C., Przybylski, M., Pompe, W., Roedel, G. (2004) In-gel screening of phosphorus and copper, zinc and iron in proteins of yeast mitochondria by LA-ICP-MS and identification of phosphory-lated protein structures by MALDI-FT-ICR-MS after separation with two-dimensional gel electrophoresis. J Anal At Spectrom, 19, 1236-1243. 

Simulation of the EMR Spectra of High-Spin Iron in Proteins... 

Gaffney BJ, Silverstone HJ. 1993. Simulation of the EMR spectra of high-spin iron in proteins. In EMR of paramagnetic molecules, pp. 1-57. Ed LJ Berliner, J Reuben. Biological magnetic resonance, Vol. 13. New York London Plenum. 

Figure 8.39 shows some results of EXAFS following absorption by iron atoms in proteins with three prototype iron-sulphur active sites. In the example in Figure 8.39(a) application of a 0.9-3.5 A filter window before Fourier retransformation shows a single wave resulting... 

Iron Sulfur Compounds. Many molecular compounds (18—20) are known in which iron is tetrahedraHy coordinated by a combination of thiolate and sulfide donors. Of the 10 or more stmcturaHy characterized classes of Fe—S compounds, the four shown in Figure 1 are known to occur in proteins. The mononuclear iron site REPLACE occurs in the one-iron bacterial electron-transfer protein mbredoxin. The [2Fe—2S] (10) and [4Fe—4S] (12) cubane stmctures are found in the 2-, 4-, and 8-iron ferredoxins, which are also electron-transfer proteins. The [3Fe—4S] voided cubane stmcture (11) has been found in some ferredoxins and in the inactive form of aconitase, the enzyme which catalyzes the stereospecific hydration—rehydration of citrate to isocitrate in the Krebs cycle. In addition, enzymes are known that contain either other types of iron sulfur clusters or iron sulfur clusters that include other metals. Examples include nitrogenase, which reduces N2 to NH at a MoFe Sg homocitrate cluster carbon monoxide dehydrogenase, which assembles acetyl-coenzyme A (acetyl-CoA) at a FeNiS site and hydrogenases, which catalyze the reversible reduction of protons to hydrogen gas. 

The most conspicuous use of iron in biological systems is in our blood, where the erythrocytes are filled with the oxygen-binding protein hemoglobin. The red color of blood is due to the iron atom bound to the heme group in hemoglobin. Similar heme-bound iron atoms are present in a number of proteins involved in electron-transfer reactions, notably cytochromes. A chemically more sophisticated use of iron is found in an enzyme, ribo nucleotide reductase, that catalyzes the conversion of ribonucleotides to deoxyribonucleotides, an important step in the synthesis of the building blocks of DNA. 

Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)...

Wachtershanser has also suggested that early metabolic processes first occurred on the surface of pyrite and other related mineral materials. The iron-sulfur chemistry that prevailed on these mineral surfaces may have influenced the evolution of the iron-sulfur proteins that control and catalyze many reactions in modern pathways (including the succinate dehydrogenase and aconitase reactions of the TCA cycle). 

All these intermediates except for cytochrome c are membrane-associated (either in the mitochondrial inner membrane of eukaryotes or in the plasma membrane of prokaryotes). All three types of proteins involved in this chain— flavoproteins, cytochromes, and iron-sulfur proteins—possess electron-transferring prosthetic groups. 

Other non-haem proteins, distinct from the above iron-sulfur proteins are involved in the roles of iron transport and storage. Iron is absorbed as Fe" in the human duodenum and passes into the blood as the Fe protein, transferrin, The Fe is in a distorted octahedral environment consisting of 1 x N, 3x0 and a chelating carbonate ion which... 

Nothing is known about the identity of the iron species responsible for dehydrogenation of the substrate. Iron-oxo species such as FeIV=0 or Fem-OOH are postulated as the oxidants in most heme or non-heme iron oxygenases. It has to be considered that any mechanistic model proposed must account not only for the observed stereochemistry but also for the lack of hydroxylation activity and its inability to convert the olefinic substrate. Furthermore, no HppE sequence homo-logue is to be found in protein databases. Further studies should shed more light on the mechanism with which this unique enzyme operates. 

When induced in macrophages, iNOS produces large amounts of NO which represents a major cytotoxic principle of those cells. Due to its affinity to protein-bound iron, NO can inhibit a number of key enzymes that contain iron in their catalytic centers. These include ribonucleotide reductase (rate-limiting in DNA replication), iron-sulfur cluster-dependent enzymes (complex I and II) involved in mitochondrial electron transport and cis-aconitase in the citric acid cycle. In addition, higher concentrations of NO,... 

Iron electronic configurations in proteins studies by Mossbauer spectroscopy. A. J. Bearden and W. R. Dunham, Struct. Bonding (Berlin), 1970, 8, 2-52 (196). 

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