Clostridium cluster

Zwielehner J, Liszt K, Handschur M, Lassl C, Lapin A, Haslberger AG. Combined PCR-DGGE fingerprinting and quantitative-PCR indicates shifts in fecal population sizes and diversity of Bacteroides, bifidobacteria and Clostridium cluster IV in institutionalized elderly. 

During the 1960s, research on proteins containing iron—sulfur clusters was closely related to the field of photosynthesis. Whereas the first ferredoxin, a 2[4Fe-4S] protein, was obtained in 1962 from the nonphotosynthetic bacterium Clostridium pasteurianum (1), in the same year, a plant-type [2Fe-2S] ferredoxin was isolated from spinach chloroplasts (2). Despite the fact that members of this latter class of protein have been reported for eubacteria and even archaebacteria (for a review, see Ref. (3)), the name plant-type ferredoxin is often used to denote this family of iron—sulfur proteins. The two decades... 

The [FeFe]-hydrogenases have been known since the 1930s [305], and Warburg recognized sulfur-coordinate iron as an essential element of the enzyme [306]. The [FeFe]-hydrogenase from Clostridium pasteurianum accommodates 20 iron atoms organized in one [2Fe-2S] cluster, three [4Fe S] clusters and the so-called H-cluster which is a [4Fe-4S] cluster covalently linked to a dinuclear [FeFe]... 

Recently Jensen and co-workers have determined the structure of a clostridial-type ferredoxin obtained from Micrococcus aerogenes (47). One of the two apparently identical iron-sulfur clusters is illustrated in Fig. 2. The structure is compatible with a model with iron and labile sulfide at alternate comers of a cube. This accounts for the equivalence of these moieties in the protein. Another 8-iron-8 labile sulfur ferredoxin, from Clostridium acidiurici, similarly contains two independent iron-sulfur clusters per molecule (48). Strahs and Kraut (49) had earlier discovered... 

Adams, M. W., Eccleston, E. and Howard, J. B. (1989) Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum. Proc. Natl. Acad. Sci. USA, 86, 4932-6. 

Erbes, D. L., Burris, R. H. and Orme-Johnson, W. H. (1975) On the iron-sulfur cluster in hydrogenase from Clostridium pasteurianum W5. Proc. Natl. Acad. Sci. USA, 72, 4795-9. 

Achim C, Golinelli M-P, Bomiaaar EL, et al. 1996. Mossbauer study of Cys56Ser mutant 2Fe ferredoxin from Clostridium pasteuriemum evidence for double exchange in an [Fc2S2] cluster. J Am Chem Soc 118 8168-9. 

Crouse BR, Meyer J, Johnson MJ. 1995. Spectroscopic evidence for a reduced Fe2S2 cluster with a S = 9/2 ground state in mutant forms of Clostridium pasteurianum 2Fe ferredoxin. J Am Chem Soc 117 9612-13. 

Das A, Coulter ED, Kurtz DM, Jr, Ljungdahl LG. 2001. Five-gene cluster in Clostridium thermo aceticum consisting of two divergent operons encoding rubredoxin oxidoreductase— rubredoxin and rubrerythrin— type A flavoprotein— high-molecular-weight rubredoxin. J Bacteriol 183 1560-7. 

Dineen, S.S., Bradshaw, M. and Johnson, E.A., Neurotoxin gene clusters in Clostridium botulinum type A strains sequence comparison and evolutionary implications, Curr. Microbiol., 46, 345-352, 2003. 

Within the cellulosome complex, type I dockerin domain is responsible for incorporating its associated glycosyl hydrolase in the bacterial cellulosome via interaction with a reception domain, the cohesin domain. The three-dimensional solution structure of the 69-residue dockerin domain from the thermophilic Clostridium thermocellum (Topt = 55-65 °C) was solved by NMR and was found to consist of two Ca " -binding loop-helix motifs connected by a linker. Each Ca " -binding subdomain is stabilized by a cluster of buried hydrophobic sidechains. Recently, the NMR sequence-specific resonance assignment of type II cohesin module from C. thermocellum has been published. ... 

Chlorophyll, and photosynthenc reaction center. 917-919 Chromium carbonyl complexes, bond lengths in, 427 Circular dichrotsm ICD). 496-499 Claasen, H. H., 70 Clathrate compounds, 304-306 Claihro-chelates, 530 Clays. 750 Clementi, E., 31, 32 Closo structures, 798-800. 807 Clostridium pasieurianttm, 934 Clusters, 738, 807-819 Coenzyme, 919 Coenzymes, vitamin B,-,... 

The bacterial ferredoxins from Peptococcus, Clostridium (Fig. 16-16B),267/268 Desulfovibrio, and other anaerobes each contain two Fe4S4 clusters with essentially the same structure as that of the Chromatium HIPIP.267 269 Each cluster can accept one electron. 

Figure 16-16 (A) Superimposed stereoscopic a-carbon traces of the peptide chain of rubredoxin from Clostridium pasteurianum with either Fe3+ (solid circles) or Zn2+ (open circles) bound by four cysteine side chains. From Dauter et al.27i (B) Alpha-carbon trace for ferredoxin from Clostridium, acidurici. The two Fe4S4 clusters attached to eight cysteine side chains are also shown. The open circles are water molecules. Based on a high-resolution X-ray structure by Duee et al.267 Courtesy of E. D. Duee. (C) Polypeptide chain of a chloroplast-type ferredoxin from the cyanobacterium Spirulina platensis. The Fe2S2 cluster is visible at the top of the molecule. From Fukuyama et al.276 Courtesy of K. Fukuyama.

More important than the demonstration (107) of nitrosylation of synthetic model clusters is the demonstration (108) of nitrosylation by nitrite of the [4Fe-4S] center in vegetative cells of Clostridium botulinum. Treatment of a reduced culture of C. botulinum with nitrite in the presence of ascorbate resulted in loss of the ESR signal at g = 1.94, characteristic of the reduced iron-sulfur protein, and its replacement by a signal at g — 2.035, characteristic of [Fe(NO)2X2] complexes, most likely of the [Fe(NO)2(SR)2] type. 

---