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Clostridial Iron-Sulphur Proteins J. Mol. Microbiol. Biotechnol. (2000) 2(1): 9-14. FermentationClostridial Symposium Fe-S Proteins 9 JMMB Minireview Clostridial Iron-Sulphur Proteins Jacques Meyer* The aim of this review is twofold: first, to point out the importance of Fe-S proteins in clostridial metabolism, and Département de Biologie Moléculaire et Structurale, second, to show that clostridia, as efficient and versatile CEA-Grenoble, 38054 Grenoble, France synthesizers of Fe-S proteins, provide a cornucopia of information on the structure and function of these proteins in all kinds of organisms. Abstract Rubredoxins Iron-sulfur proteins are ubiquitous catalysts of a wide range of biological reactions, and are particularly As the simplest of all Fe-S proteins, rubredoxins from abundant in clostridia which lack the ability to anaerobic bacteria comprise 45 to 54 residues, and their synthesize hemes. The development of research on active site consists of a single iron coordinated to four these metalloproteins has therefore been strongly cysteinyl sulfurs. Rubredoxin-encoding genes have been associated with biochemical investigations of found in C. pasteurianum (Mathieu et al., 1992), clostridial metabolism. Major breakthroughs in the C. beijerinckii (Wilkinson and Young, 1995), C. perfringens field, from the first isolation of an iron-sulfur protein (Katayama et al., 1995), C. acetobutylicum (Cornillot et al., in 1962, to the recent determination of an Fe- 1997), and C. butyricum (Gérard et al., 1999). At least four hydrogenase structure, have been made with primary structures (C. pasteurianum, C.perfringens, clostridia. These data, as well as others obtained C. sticklandii, and C. thermosaccharolyticum) of clostridial through studies on clostridia, are transferable to many rubredoxins have been determined either by protein or by other bioenergetic machineries, due to the strong DNA sequencing (reviewed in Mathieu et al., 1992). phylogenetic conservation of some important The monocistronic C. pasteurianum rubredoxin gene components. For instance, clear homologies exist has been cloned, sequenced, and expressed in E. coli between constituents of the anaerobic electron (Mathieu et al., 1992; Mathieu and Meyer, 1993). Both the transfer chains in clostridia and aerobic respiratory native-like Fe-containing and a Zn-substituted forms of the chains. The contribution of iron-sulfur proteins to the protein have thus been isolated and structurally biotechnological and medical significance of clostridia characterized (Dauter et al., 1996). The heterologous is also discussed. Structural and functional genomics expression system has allowed isotopic labeling of C. are expected to bring forth a wealth of novel data on pasteurianum rubredoxin and assignment of previously clostridia and iron-sulfur proteins. unobserved NMR resonances of the cysteine ligands of the iron (Xia et al., 1995). Many mutated forms of rubredoxin Introduction have been prepared with the aims of understanding the stability (Eidsness et al., 1997) and the electron transfer Iron-sulfur (Fe-S) proteins contain active sites consisting properties of this protein (Kümmerle et al., 1997) or of variable numbers (one to eight) of inorganic sulfide assembling novel metal sites (Meyer et al., 1995; 1997; (S2-) and iron atoms bound to the polypeptide chain by Xiao et al., 1998). cysteinyl sulfur atoms (Johnson, 1994 ; Beinert et al., 1997). The yet unknown function of rubredoxins in clostridia In some rare cases histidine ligation has been observed might be analogous to the one hypothesized in sulfate (Moulis et al. 1996 ; see section on hydrogenase below). reducing bacteria, namely a possible involvement in the The fact that Fe-S proteins are ubiquitous catalysts and protection against oxygen (Voordouw and Voordouw, regulators in living cells may be related to a possible role 1998). of iron-sulfur chemistry in the origin of life (Huber and Wächtershäuser, 1998; Russell and Hall, 1997). These [2Fe-2S] Ferredoxin proteins are particularly abundant and diverse in clostridia which lack the heme synthesis machinery. For This protein (Hardy et al., 1965) has been sequenced and circumstantial reasons, in particular early studies on the characterized by various spectroscopic techniques biochemistry of nitrogen fixation (Carnahan et al., 1960; (reviewed in Meyer et al., 1994). It is a dimer of a 102- Mortenson et al., 1962; Hardy et al., 1965), Clostridium residue polypeptide chain containing one [2Fe-2S] cluster pasteurianum is, among clostridia, the best source of well per subunit. The encoding gene is monocistronic (Meyer, characterized Fe-S proteins. However, most of the data 1993) and has been expressed in E. coli (Fujinaga and can be extrapolated to other clostridia, including the Meyer, 1993). Unique structural features of this protein have pathogens and those of biotechnological significance. been uncovered by site-directed mutagenesis (Meyer et al., 1994 ; Golinelli et al., 1996 ; 1998). Molecular variants Abbreviations with cysteine ligands of the Fe-S cluster substituted with Fe-S: iron sulfur; H2ase: hydrogenase; PFOR: pyruvate-ferredoxin serine (Fujinaga et al., 1993 ; Meyer et al., 1994) have oxidoreductase. allowed the discovery of novel properties of [2Fe-2S] active Received October 06, 1999; revised October 12, 1999; accepted October sites (Crouse et al., 1995 ; Achim et al., 1996 ; 1999). 12, 1999. *For correspondence. Email [email protected]; Tel. +33-476884423; Fax. +33-476885872. © 2000 Horizon Scientific Press Further Reading Caister Academic Press is a leading academic publisher of advanced texts in microbiology, molecular biology and medical research. 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It appears to have acetylCoA and reducing the 2[4Fe-4S] ferredoxin. no counterparts in other members of the genus Clostridium Clostridial PFORs are homodimers
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