Clostridium pasteurianum

RB Yelle, N-S Park, T Ichiye. Molecular dynamics simulations of rubredoxm from Clostridium pasteurianum Changes m structure and electrostatic potential during redox reactions. Proteins 22 154-167, 1995. 

I Qumkal, V Davasse, 1 Gaillard, J-M Mouhs. On the role of conserved prohne residues in the structure and function of Clostridium pasteurianum 2[4Ee-4S] ferredoxm. Protein Eng 7 681-687, 1994. 

Q Zeng, ET Smith, DM Kurtz, RA Scott. Protein determinants of metal site reduction potentials. Site directed mutagenesis studies of Clostridium pasteurianum laibredoxin. Inorg Chim Acta 242 245-251, 1996. 

Fig. 2. H NMR spectra of (A) oxidized spinach Fe2S2 ferredoxin (33) (B) reduced spinach Fe2S2 ferredoxin (5f) (C) oxidized Desulfovibrio gigas Fe3S4 ferredoxin (138) (D) oxidized ectothiorhodospira halophila HiPIP iso-II (23) (E) reduced Chromatium vinosum HiPIP (14) (F) fully reduced Clostridium pasteurianum 2(Fe4S4) ferredoxin (139). Chemical shift values are in ppm.

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... 

Fig. 10. Comparison between the g values of Cys-to-Ser mutants and wild-type [2Fe-2S] proteins, in cases where the substitution takes place at (A) the reducible site Emd (B) the nom-educible site. The following symbols indicate the various proteins , Anahaena 7120 vegetative ferredoxin , human ferredoxin , Frd B subunit in E. coli fumEirate reductase , Clostridium pasteurianum ferredoxin. Filled and empty symbols indicate the wild-t3ipe and mutant proteins, respectively.

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]... 

FeFe]-hydrogenase and models HRed. Clostridium pasteurianum 4.2 0.08 0.87 [310]... 

This review will not be concerned with functionally alternative structures and metabolites which appear in iron-limited growth. Thus Clostridium pasteurianum and other bacteria when grown in the presence of iron form ferredoxin grown at low iron the same organisms form flavodoxin, a flavoprotein [Knight, ., Jr., Hardy, R. W. J. Biol. Chem. 242, 1370 (1967) Mayhem, S. G., Massey, V. J. Biol. Chem. 244, 794 (1969)]. 

The crystallographic structure of rubredoxin from Clostridium pasteurianum at 2.5 A, a resolution sufficient to reveal the sequence of several of the bulky amino acid side chains, shows the iron coordinated to two pairs of cysteine residues located rather near the termini of the polypeptide chain (Fig. 1). A related rubredoxin, with a three times larger molecular weight, from Pseudomonas oleovorans is believed to bind iron in a similar fashion. This conclusion is based on physical probes, especially electron paramagnetic resonance spectroscopy, all of which indicate that the iron is in each case situated in a highly similar environment however, the proteins display some specificity in catalytic function. 

Fig. 1. The iron-cysteinyl center of Clostridium pasteurianum rubredoxin (45). Two centers of this type are proposed to occur in Pseudomonas oleovarans rubredoxin 46)...

JW. Peters, WN. Lanzilotta, BJ. Lemon, LC. eefeldt (1998) X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom resolution. Science, 282 1853-1858... 

The simplest of these proteins are rubredoxins, which are bacterial proteins having a characteristic red colour (from which their name is derived) containing an FeS4 assembly, consisting of an Fe(III) ion coordinated to four cysteine groups. The typical tetrahedral structure of this group is illustrated in Figure 17 for the rubredoxin isolated from Clostridium pasteurianum (FW 6100).35... 

Figure 17 X-Ray structure of the active site of the rubredoxin from Clostridium pasteurianum...

Figure 18 Cyclic voltammograms recorded at an edge-oriented pyrolitic graphite electrode in an aqueous solution (pH 8) of the rubredoxin from Clostridium pasteurianum. In the absence (a) and in the presence (b) of [Cr(NH3)6J3+. Scan rate 0.02 V s J...

We tried preparations from a variety of N2-fixing agents, but responses were variable. Sometimes we achieved rather good fixation with cell-free preparations, but the results were not consistent. For example, at a meeting in early 1958, we reported that cell-free preparations from Clostridium pasteurianum exposed under an atmo-... 

Mortenson, L.E. Nitrogen fixation in extracts of Clostridium pasteurianum. In Non-heme Iron Proteins Role in Energy Conversion,... 

Tso, M.-Y., T. Ljones and R.H. Burris. Purification of the nitrogenase protein from Clostridium pasteurianum. Biochim. Biophys. Acta 267,600-604 (1972). 

McNary, J.H. and R.H. Burris. Energy requirements for nitrogen fixation by cell-free preparations from Clostridium pasteurianum. J. Bacterid. 84, 598-599 (1962). 

These are classically represented by the enzymes from obligate anaerobes including the sulfate reducer D. vulgaris (Vourdouw and Brenner 1985) and the saccharolytic Clostridium pasteurianum (Meyer and Gagnon 1991) in which the enzymes act in uptake or evolution modes respectively. Many examples are a (3 heterodimers like the NiFe-membrane or periplasmic enzymes yet the primary sequences of the subunits of... 

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. 

Lemon, B. J. and Peters, J. W. (1999) Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum. Biochemistry, 38, 12969-73. 

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. 

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