메뉴 건너뛰기




Volumn 271, Issue 6, 2004, Pages 1106-1116

Two distinct heterodisulfide reductase-like enzymes in the sulfate-reducing archaeon Archaeoglobus profundus

Author keywords

Archaeoglobus; Heterodisulfide reductase; Hmc complex; Iron sulfur proteins; Sulfate reducing bacteria

Indexed keywords

CYTOCHROME B; DISULFIDE; HETERODISULFIDE REDUCTASE; HYDROGENASE; IRON; IRON SULFUR PROTEIN; NICKEL; OXIDOREDUCTASE; SULFATE; SULFUR; UNCLASSIFIED DRUG;

EID: 1642295867     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04013.x     Document Type: Article
Times cited : (61)

References (41)
  • 1
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer, R.K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144, 2377-2406.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 2
    • 0025187801 scopus 로고
    • Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
    • Hedderich, R., Berkessel, A. & Thauer, R.K. (1990) Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 193, 255-261.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 255-261
    • Hedderich, R.1    Berkessel, A.2    Thauer, R.K.3
  • 3
    • 0028136101 scopus 로고
    • The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine nucleotide-dependent thioredoxin reductases
    • Hedderich, R., Koch, J., Linder, D. & Thauer, R.K. (1994) The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine nucleotide-dependent thioredoxin reductases. Eur. J. Biochem. 225, 253-261.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 253-261
    • Hedderich, R.1    Koch, J.2    Linder, D.3    Thauer, R.K.4
  • 4
    • 0028351576 scopus 로고
    • Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri
    • Heiden, S., Hedderich, R., Setzke, E. & Thauer, R.K. (1994) Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri. Eur. J. Biochem. 221, 855-861.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 855-861
    • Heiden, S.1    Hedderich, R.2    Setzke, E.3    Thauer, R.K.4
  • 5
    • 0031055712 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme
    • Künkel, A., Vaupel, M., Heim, S., Thauer, R.K. & Hedderich, R. (1997) Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme. Eur. J. Biochem. 244, 226-234.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 226-234
    • Künkel, A.1    Vaupel, M.2    Heim, S.3    Thauer, R.K.4    Hedderich, R.5
  • 6
    • 0032516483 scopus 로고    scopus 로고
    • Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila
    • Simianu, M., Murakami, E., Brewer, J.M. & Ragsdale, S.W. (1998) Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila. Biochemistry. 37, 10027-10039.
    • (1998) Biochemistry , vol.37 , pp. 10027-10039
    • Simianu, M.1    Murakami, E.2    Brewer, J.M.3    Ragsdale, S.W.4
  • 7
    • 0034858150 scopus 로고    scopus 로고
    • A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea
    • Madadi-Kahkesh, S., Duin, E.C., Heim, S., Albracht, S.P.J., Johnson, M.K. & Hedderich, R. (2001) A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. Eur. J. Biochem. 268, 2566-2577.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2566-2577
    • Madadi-Kahkesh, S.1    Duin, E.C.2    Heim, S.3    Albracht, S.P.J.4    Johnson, M.K.5    Hedderich, R.6
  • 8
    • 0037070204 scopus 로고    scopus 로고
    • Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction
    • Duin, E.C., Madadi-Kahkesh, S., Hedderich, R., Clay, M.D. & Johnson, M.K. (2002) Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction. FEBS Lett. 512, 263-268.
    • (2002) FEBS Lett. , vol.512 , pp. 263-268
    • Duin, E.C.1    Madadi-Kahkesh, S.2    Hedderich, R.3    Clay, M.D.4    Johnson, M.K.5
  • 10
    • 0032586857 scopus 로고    scopus 로고
    • 2: Heterodisulfide oxidoreductase from Methanosarcina mazei Göl: Identification of two proton-translocating segments
    • 2: heterodisulfide oxidoreductase from Methanosarcina mazei Göl: Identification of two proton-translocating segments. J. Bacteriol. 181, 4076-4080.
    • (1999) J. Bacteriol. , vol.181 , pp. 4076-4080
    • Ide, T.1    Bäumer, S.2    Deppenmeier, U.3
  • 12
    • 0028177028 scopus 로고
    • 2: Heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties
    • 2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties. Eur. J. Biochem. 220, 139-148.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 139-148
    • Setzke, E.1    Hedderich, R.2    Heiden, S.3    Thauer, R.K.4
  • 14
    • 85047695985 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea
    • Mander, G.J., Duin, E.C., Linder, D., Stetter, K.O. & Hedderich, R. (2002) Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea. Eur. J. Biochem. 269, 1895-1904.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1895-1904
    • Mander, G.J.1    Duin, E.C.2    Linder, D.3    Stetter, K.O.4    Hedderich, R.5
  • 18
    • 0027323851 scopus 로고
    • The hmc-operon of Desulfovibrio vulgar is subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex
    • Rossi, M., Pollock, W.B., Reij, M.W., Keon, R.G., Fu, R. & Voordouw, G. (1993) The hmc-operon of Desulfovibrio vulgar is subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex. J. Bacteriol. 175, 4699-4711.
    • (1993) J. Bacteriol. , vol.175 , pp. 4699-4711
    • Rossi, M.1    Pollock, W.B.2    Reij, M.W.3    Keon, R.G.4    Fu, R.5    Voordouw, G.6
  • 19
    • 0028902975 scopus 로고
    • 2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
    • 2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus. Arch. Microbiol. 163, 112-118.
    • (1995) Arch. Microbiol. , vol.163 , pp. 112-118
    • Vorholt, J.1    Kunow, J.2    Stetter, K.O.3    Thauer, R.K.4
  • 20
    • 0025274687 scopus 로고
    • Archaeoglobus profundus sp. nov., represents a new species within sulfate-reducing archaea
    • Burggraf, S., Jannasch, H.W., Nicolaus, B. & Stetter, K.O. (1990) Archaeoglobus profundus sp. nov., represents a new species within sulfate-reducing archaea. Syst. Appl. Microbiol. 13, 24-28.
    • (1990) Syst. Appl. Microbiol. , vol.13 , pp. 24-28
    • Burggraf, S.1    Jannasch, H.W.2    Nicolaus, B.3    Stetter, K.O.4
  • 21
    • 0020494651 scopus 로고
    • New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria
    • Beinert, H. & Albracht, S.P. (1982) New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochim. Biophys. Acta. 683, 245-277.
    • (1982) Biochim. Biophys. Acta. , vol.683 , pp. 245-277
    • Beinert, H.1    Albracht, S.P.2
  • 22
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish, W.W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 158, 357-364.
    • (1988) Methods Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 23
    • 84944816274 scopus 로고
    • Spectrophotometric determination of hydrogen sulfide in natural waters
    • Cline, J.D. (1969) Spectrophotometric determination of hydrogen sulfide in natural waters. Limnol. Oceanogr. 14, 454-458.
    • (1969) Limnol. Oceanogr. , vol.14 , pp. 454-458
    • Cline, J.D.1
  • 24
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the bradford protein assay increases its sensitivity - Theoretical and experimental studies
    • Zor, T. & Seliger, Z. (1996) Linearization of the bradford protein assay increases its sensitivity - theoretical and experimental studies. Anal. Biochem. 236, 302-308.
    • (1996) Anal. Biochem. , vol.236 , pp. 302-308
    • Zor, T.1    Seliger, Z.2
  • 25
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b and c from pyridine hemochrome spectra
    • Berry, E.A. & Trumpower, B.L. (1987) Simultaneous determination of hemes a, b and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 26
    • 0018068050 scopus 로고
    • Bacterial cytochromes and their spectral characterization
    • Smith, L. (1978) Bacterial cytochromes and their spectral characterization. Methods Enzymol. 53, 202-212.
    • (1978) Methods Enzymol. , vol.53 , pp. 202-212
    • Smith, L.1
  • 27
    • 0020624680 scopus 로고
    • 2 oxidoreductase from Rhodopseudomonas sphaeroides GA
    • 2 oxidoreductase from Rhodopseudomonas sphaeroides GA. FEBS Lett. 153, 146-150.
    • (1983) FEBS Lett. , vol.153 , pp. 146-150
    • Gabellini, N.1    Hauska, G.2
  • 28
    • 0025917055 scopus 로고
    • The heme groups of cytochrome o from Escherichia coli
    • Puustinen, A. & Wikström, M. (1991) The heme groups of cytochrome o from Escherichia coli. Proc. Natl Acad. Sci. USA 88, 6122-6126.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6122-6126
    • Puustinen, A.1    Wikström, M.2
  • 29
    • 0018785560 scopus 로고
    • Intensity of highly anisotropic low-spin heme EPR signals
    • de Vries, S. & Albracht, S.P. (1979) Intensity of highly anisotropic low-spin heme EPR signals. Biochim. Biophys. Acta. 546, 334-340.
    • (1979) Biochim. Biophys. Acta. , vol.546 , pp. 334-340
    • De Vries, S.1    Albracht, S.P.2
  • 32
    • 0002918710 scopus 로고
    • Electron-paramagnetic resonance studies on flavoprotein radicals
    • Kamin, H., ed. University Park Press, Baltimore, MD
    • Palmer, G., Müller, F. & Massey, V. (1971) Electron- paramagnetic resonance studies on flavoprotein radicals. Flavins and Flavoproteins (Kamin, H., ed.), pp. 123-137. University Park Press, Baltimore, MD.
    • (1971) Flavins and Flavoproteins , pp. 123-137
    • Palmer, G.1    Müller, F.2    Massey, V.3
  • 33
    • 0032263876 scopus 로고    scopus 로고
    • Iron-sulfur clusters and their electronic and magnetic properties
    • Mouesca, J.-M. & Lamotte, B. (1998) Iron-sulfur clusters and their electronic and magnetic properties. Coordin. Chem. Rev. 178-180, 1573-1614.
    • (1998) Coordin. Chem. Rev. , vol.178-180 , pp. 1573-1614
    • Mouesca, J.-M.1    Lamotte, B.2
  • 34
    • 0000415615 scopus 로고    scopus 로고
    • Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins
    • Hill, H.A.O., Sadler, P.J. & Thomson, A.J., eds. Springer Verlag, Berlin
    • Capozzi, F., Ciurli, S. & Luchinat, C. (1998) Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins. Structure Bonding (Hill, H.A.O., Sadler, P.J. & Thomson, A.J., eds), pp. 127-160. Springer Verlag, Berlin.
    • (1998) Structure Bonding , pp. 127-160
    • Capozzi, F.1    Ciurli, S.2    Luchinat, C.3
  • 35
    • 0034846069 scopus 로고    scopus 로고
    • Spectroscopic and model studies of the Ni-Fe hydrogenase reaction mechanism
    • Maroney, M.J. & Bryngelson, P.A. (2001) Spectroscopic and model studies of the Ni-Fe hydrogenase reaction mechanism. J. Biol. Inorg. Chem. 6, 453-459.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 453-459
    • Maroney, M.J.1    Bryngelson, P.A.2
  • 36
    • 0031921345 scopus 로고    scopus 로고
    • Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Göl
    • Abken, H.J., Tietze, M., Brodersen, J., Bäumer, S., Beifuss, U. & Deppenmeier, U. (1998) Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Göl. J. Bacteriol. 180, 2027-2032.
    • (1998) J. Bacteriol. , vol.180 , pp. 2027-2032
    • Abken, H.J.1    Tietze, M.2    Brodersen, J.3    Bäumer, S.4    Beifuss, U.5    Deppenmeier, U.6
  • 37
    • 0028890441 scopus 로고
    • Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain G1, both encoding a membrane-bound hydrogenase and a cytochrome b
    • Deppenmeier, U., Blaut, M., Lentes, S., Herzberg, C. & Gottschalk, G. (1995) Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain G1, both encoding a membrane-bound hydrogenase and a cytochrome b. Eur. J. Biochem. 227, 261-269.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 261-269
    • Deppenmeier, U.1    Blaut, M.2    Lentes, S.3    Herzberg, C.4    Gottschalk, G.5
  • 39
    • 0000132043 scopus 로고
    • A novel fully saturated menaquinone from the thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus
    • Tindall, B.J., Stetter, K.O. & Coffins, M.D. (1989) A novel fully saturated menaquinone from the thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus. J. Gen. Microbiol. 135, 693-696.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 693-696
    • Tindall, B.J.1    Stetter, K.O.2    Coffins, M.D.3
  • 41
    • 0038782226 scopus 로고    scopus 로고
    • Gene expression analysis of energy metabolism mutants of Desulfovibrio vulgaris Hildenborough indicates an important role for alcohol dehydrogenase
    • Haveman, S.A., Brunelle, V., Voordouw, J.K., Voordouw, G., Heidelberg, J.F. & Rabus, R. (2003) Gene expression analysis of energy metabolism mutants of Desulfovibrio vulgaris Hildenborough indicates an important role for alcohol dehydrogenase. J. Bacteriol. 185, 4345-4353.
    • (2003) J. Bacteriol. , vol.185 , pp. 4345-4353
    • Haveman, S.A.1    Brunelle, V.2    Voordouw, J.K.3    Voordouw, G.4    Heidelberg, J.F.5    Rabus, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.