Abstract
Periplasmic extract from Desulfovibrio desulfuricans (NCIMB 8372) was found to contain two different c-type cytochromes. One is tetraheme cytochrome c3 and the other is monoheme cytochrome c553. Cytochrome c3 could be purified by a procedure involving only one chromatographic step, whereas cytochrome c553 required several such steps. Cytochrome c3 was found to have a relative molecular mass of 14300 and an isoionic point higher than 9. Analysis of the redox potentials indicated one heme at -260 mV and three hemes around -330 mV. Cytochrome c553 had a relative molecular mass of 7200, an isoionic point higher than 9 and a redox potential of 0 mV.
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References
BellGR, LeGallJ, PeckHDJr (1974) Evidence for the periplasmic location of hydrogenase in Desulfovibrio gigas. J Bacteriol 120: 994–997
BiancoP, HaladjianJ, PilardR (1982) Electrochemistry of c-type cytochromes. Electrode reactions of cytochrome c553 from Desulfovibrio vulgaris Hildenborough. J Electroanal Chem 136: 291–299
BradfordMM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254
DollaA, BruschiM (1988) The cytochrome c3-ferredoxin electron transfer complex: cross-linking studies. Biochim Biophys Acta 932: 26–32
DruckerH, TrousilEB, CampbellLL (1970) Purification and properties of cytochrome c3 of Desulfovibrio salexigens. Biochemistry 9: 3395–3400
FauqueG, BruschiM, LeGallJ (1979) Purification and some properties of cytochrome c553(550) isolated from Desulfovibrio desulfuricans Norway. Biochem Biophys Res Commun 86: 1020–1029
GoodhewCF, BrownKR, PettigrewGW (1986) Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes. Biochim Biophys Acta 852: 288–294
HatchikianEC, PapavassiliouP, BiancoP, HaladjianJ (1984) Characterization of cytochrome c3 from the thermophilic sulfate reducer Thermodesulfobacterium commune. J Bacteriol 159: 1040–1046
HorioT, KamenMD (1961) Preparation and properties of three pure crystaline bacterial haem proteins. Biochim Biophys Acta 48: 266–286
IshimotoM, KoyamaJ, NagaiY (1954) Biochemical studies on sulfate-reducing bacteria. IV. The cytochrome system of sulfate-reducing bacteria. J Biochem Tokyo 41: 763–770
KramerJF, PopeDH, SalernoJC (1986) Purification and characterization of low potential c cytochromes from Desulfovibrio desulfuricans membranes. FEBS Lett 206: 157–161
LeGallJ, ForgetN (1978) Purification of electron-transfer components from sulfate-reducing bacteria. In: FleischerS, PackerL (eds) Methods in enzymology. vol 53. Academic Press, New York San Francisco London, pp 613–653
LeGallJ, PeckHDJr (1987) Amino-terminal amino acid sequences of electron transfer proteins from gram-negative bacteria as indicators of their cellular localization: the sulfate-reducing bacteria. FEMS Microbiol Rev 46: 35–40
LeGallJ, MazzaG, DragoniN (1965) Le cytochrome c3 de Desulfovibrio gigas. Biochim Biophys Acta 99: 385–387
MayhewSG, DijkCvan, WestenHMvan der (1978) Properties of hydrogenases from the anaerobic bacteria Megasphaera elsdenii and Desulfovibrio vulgaris (Hildenborough). In: SchlegelHG, SchneiderK (eds) Hydrogenases: Their catalytic activity, structure and function. Erich Goltze KG, Göttingen, pp 125–140
MouraI, FauqueG, LeGallJ, XavierAV, MouraJJG (1987) Characterization of the cytochrome system of a nitrogen-fixing strain of a sulfate-reducing bacterium: Desulfovibrio desulfuricans Berre-Eau. Eur J Biochem 162: 547–554
OgataM, KondoS, OkawaraN, YagiT (1988) Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki. J Biochem 103: 121–125
PeckHDJr, LeGallJ (1982) Biochemistry of dissimilatory sulphate reduction. Phil Trans R Soc Lond B 298: 443–466
PostgateJR (1954) Presence of cytochrome in an obligate anaerobe. Biochem J 56: XI-XII
PostgateJR (1984) The sulphate-reducing bacteria. Cambridge University Press, Cambridge
SingletonRJr, CampbellLL, HawkridgeFM (1979) Cytochrome c3 from the sulfate-reducing anaerobe Desulfovibrio africanus Benghazi: Purification and properties. J Bacteriol 140: 893–901
StankovichMT (1980) An anaerobic spectroelectrochemical cell for studying the spectral and redox properties of flavoproteins. Anal Biochem 109: 295–308
TakaichiS, MoritaS (1981) Procedures and conditions for application of the pyridine hemochrome method to photosynthetically grown cells of Rhodopseudomonas sphaeroides. J Biochem 89: 1513–1519
VanRooijenGJH, BruschiM, VoordouwG (1989) Cloning and sequencing of the gene encoding cytochrome c553 from Desulfovibrio vulgaris Hildenborough. J Bacteriol 171: 3575–3578
Van derWestenHM, MayhewSG, VeegerC (1978) Separation of hydrogenase from intact cells of Desulfovibrio vulgaris: Purifications and properties. FEBS Lett 86: 122–126
VoordouwG, BrennerS (1986) Cloning and sequencing of the gene encoding cytochrome c3 from Desulfovibrio vulgaris Hildenborough. Eur J Biochem 159: 347–351
WesterbergO (1972) Isoelectric focusing of proteins in polyacrylamide gels. Biochim Biophys Acta 257: 11–19
YagiT (1979) Purification and properties of cytochrome c-553, an electron acceptor for formate dehydrogenase of Desulfovibrio vulgaris, Miyazaki. Biochim Biophys Acta 548: 96–105
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Eng, L.H., Neujahr, H.Y. Purification and characterisation of periplasmic C-type cytochromes from Desulfovibrio desulfuricans (NCIMB 8372). Arch. Microbiol. 153, 60–63 (1989). https://doi.org/10.1007/BF00277542
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DOI: https://doi.org/10.1007/BF00277542