Characterization of the cytochromes C from Desulfovibrio desulfuricans G201.

A monoheme cytochrome c553 and a hexadecaheme high molecular weight cytochrome (Hmc) have been isolated and characterized from the sulfate-reducing bacteria Desulfovibrio desulfuricans G201, in addition to the tetraheme cytochrome c3 (Mr 13000) that has been previously described. Both cytochromes are homologous with respect to several biochemical properties to the corresponding cytochromes found in other Desulfovibrio species. However, they are acidic proteins while the corresponding molecules, isolated from other Desulfovibrio species, are relatively more basic. The D. desulfuricans cytochrome content appears identical to that of D. vulgaris Hildenborough. Isolation of these cytochromes from a Desulfovibrio desulfuricans strain is of great interest in order to get more insight on the physiological function of these molecules.

[1]  M. Bruschi,et al.  Amino-acid sequence of cytochrome c-553 from Desulfovibrio desulfuricans Norway. , 1993, Biochimica et biophysica acta.

[2]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[3]  M. W. Reij,et al.  The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex , 1993, Journal of bacteriology.

[4]  M. Bruschi,et al.  Biochemical and spectroscopic characterization of the high molecular weight cytochrome c from Desulfovibrio vulgaris Hildenborough expressed in Desulfovibrio desulfuricans G200. , 1992, Biochemistry.

[5]  S. Moore,et al.  The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. , 1963, The Journal of biological chemistry.

[6]  M. Bruschi,et al.  A Single Mutation in the Heme 4 Environment ofDesulfovibrio desulfuricans Norway Cytochromec 3 (M r 26,000) Greatly Affects the Molecule Reactivity* , 1997, The Journal of Biological Chemistry.

[7]  M Czjzek,et al.  Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution. , 1994, Journal of molecular biology.

[8]  F. Guerlesquin,et al.  Functional expression of Desulfovibrio vulgaris Hildenborough cytochrome c3 in Desulfovibrio desulfuricans G200 after conjugational gene transfer from Escherichia coli , 1990, Journal of bacteriology.

[9]  M. Blackledge,et al.  Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics. , 1995, Journal of Molecular Biology.

[10]  W. Hagen,et al.  Cytochrome c553 from Desulfovibrio vulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase. , 1994, European journal of biochemistry.

[11]  N. Yasuoka,et al.  Refined structure of cytochrome c3 at 1.8 A resolution. , 1984, Journal of molecular biology.

[12]  F. Guerlesquin,et al.  Amino-acid sequence of the cytochrome c3 (M(r) 26,000) from Desulfovibrio desulfuricans Norway and a comparison with those of the other polyhemic cytochromes from Desulfovibrio. , 1994, Biochimica et biophysica acta.

[13]  C. Costa,et al.  Cytochrome components of nitrate- and sulfate-respiring Desulfovibrio desulfuricans ATCC 27774 , 1988, Journal of bacteriology.

[14]  M. Bruschi.  The primary structure of the tetrahaem cytochrome c3 from Desulfovibrio desulfuricans (strain norway 4). Description of a new class of low-potential cytochrome c , 1981 .

[15]  M. Bruschi,et al.  Cloning and sequencing of the gene encoding cytochrome c553 from Desulfovibrio vulgaris Hildenborough , 1989, Journal of bacteriology.

[16]  M. Bruschi.  Cytochrome c3 (M(r) 26,000) isolated from sulfate-reducing bacteria and its relationships to other polyhemic cytochromes from Desulfovibrio. , 1994, Methods in enzymology.

[17]  M. Bruschi,et al.  Purification and some properties of cytochrome C553(550) isolated from Desulfovibrio desulfuricans Norway. , 1979, Biochemical and biophysical research communications.

[18]  T. Yagi,et al.  Characterization and redox properties of high molecular mass cytochrome c3 (Hmc) isolated from Desulfovibrio vulgaris Miyazaki. , 1993, Biochimie.

[19]  M. Bruschi,et al.  The cytochrome c3 superfamily: amino acid sequence of a dimeric octahaem cytochrome c3 (M(r) 26,000) isolated from Desulfovibrio gigas. , 1996, The Biochemical journal.

[20]  L. Seefeldt,et al.  The identification, characterization, sequencing and mutagenesis of the genes (hupSL) encoding the small and large subunits of the H2‐uptake hydrogenase of Azotobacter chroococcum , 1990, Molecular microbiology.

[21]  L. Pieulle,et al.  Biochemical studies of the c-type cytochromes of the sulfate reducer Desulfovibrio africanus. Characterization of two tetraheme cytochromes c3 with different specificity. , 1996, Biochimica et biophysica acta.

[22]  Ambler Rp.  THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551. , 1963 .

[23]  Manuela M. Pereira,et al.  Isolation and characterization of a high molecular weight cytochrome from the sulfate reducing bacterium Desulfovibrio gigas , 1994, FEBS letters.

[24]  D. J. Stewart.  The sulphate-reducing bacteria, 2nd ed.: By J. R. Postgate. Pp. 208. Cambridge University Press, 1984. £20.00 ($29.50) , 1984 .

[25]  A. Zehnder.  Biology of anaerobic microorganisms , 1988 .

[26]  F. Guerlesquin,et al.  Crystal structure of a dimeric octaheme cytochrome c3 (M(r) 26,000) from Desulfovibrio desulfuricans Norway. , 1996, Structure.

[27]  H. Akutsu,et al.  A Gene Encoding a Cytochrome c Oxidase‐Like Protein Is Located Closely to the Cytochrome c‐553 Gene in the Anaerobic Bacterium, Desulfovibrio vulgaris (Miyazaki F) , 1995, Microbiology and immunology.

[28]  R P Ambler,et al.  Sequence variability in bacterial cytochromes c. , 1991, Biochimica et biophysica acta.

[29]  H. D. Peck,et al.  Cloning and sequencing of the genes encoding the large and small subunits of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio baculatus , 1987, Journal of bacteriology.

[30]  T. Yagi.  Purification and properties of cytochrome c-553, an electron acceptor for formate dehydrogenase of Desulfovibrio vulgaris, Miyazaki. , 1979, Biochimica et biophysica acta.

[31]  M. Bruschi,et al.  Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough , 1991, Journal of bacteriology.

[32]  J. Falk,et al.  Porphyrins and Metalloporphyrins - Their General, Physical and Coordination Chemistry and Laboratory Methods , 1964 .