Iron-sulfur proteins identification

Trumpower, B. L., and Edwards, C. A., 1979, Identification of oxidation factor as a reconstitu-tively active form of the iron-sulfur protein of the cytochrome fc-Cj segment of the respiratory chain, FEB.S Lett. 100 13nl6. 

R Maikin and PJ Aparicio (1975) Identification of a g=1.90 high-potential iron-sulfur protein in chloroplasts. Biochem Biophys Res Commun 63 1157-1160... 

Holm, R.H. Identification of Active Sites in Iron-Sulfur Proteins. In Biological Aspects of Inorganic Chemistry (eds. Addison, A. W., et al.), New York, Willey Interscience Publications 1977, pp. 77-111... 

Holm, R. H. Identification of active sites in iron-sulfur proteins. In A. W. Addison et ai, Biological Aspects of Inorganic Chemistry (New York Wiley-Interscience, 1977), 71-11). 

An excellent example of the powerful combination of ENDOR with isotopic labeling studies is found in the identification of histidine ligands in the Rieske-type 2Fe-2S iron-sulfur protein of phthalate dioxygenase (PDO). As shown in Fig. 12, the X-band " N cw ENDOR spectrum of natural-abundance PDO shows a broad pattern of N resonances that by... 

The PSI-C polypeptide has a molecular mass of 9 kDa and binds the iron-sulfur clusters A and B (4). The first proposal of the PSI-C polypeptide as being an iron-sulfur protein was based on its high cysteine content (37). The protein was isolated from PS I particles of barley and shown to carry zero-valence sulfur which is indicative for a denatured iron-sulfur center (4). The amount of zero-valence sulfur bound to the polypeptide corresponded to 8 acid-labile sulfides per molecule (4). The N-terminal amino acid sequence of the isolated protein permitted the identification of its corresponding chloroplast gene which... 

Extrusion as well as reconstitution reactions appear to be an excellent tool in the identification of the active sites in numerous iron-sulfur proteins and enzymes in which the sites cannot be directly investigated. However there are some requirements for the use of this technique, e.g. protein solubility and stability under denaturing conditions, and distinctive spectral or other characteristics permitting the differentiation of the extrusion products from the halo-protein. Structural integrity of the core during and after extrusion also appears as an important condition. Indeed, in some cases it has been observed that an equilibrium dimer-tetramer can occur. 

Strain J, Lorenz CR, Bode J, et al. 1998. Supressors of superoxide dismutase (SODl) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J Biol Chem 273 31138-44. 

Orme-Johnson, W. H., Holm, R.H. Identification of Iron Sulfur Clusters in Proteins. In Methods in Enzymology, Vol. 53 (ed. Fleicher, S., Parker, L.), New York, Academic Press 1978, pp. 631-634... 

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