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Volumn 18, Issue 13, 2013, Pages 1613-1622

In the absence of thioredoxins, what are the reductants for peroxiredoxins in thermotoga maritima?

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOFERRITIN; GLUTAREDOXIN; NITROREDUCTASE; PEROXIREDOXIN; PEROXIREDOXIN 6; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 84875745916     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4739     Document Type: Review
Times cited : (10)

References (9)
  • 1
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    • DOI 10.1111/j.1462-2920.2004.00639.x
    • Ackerley DF, Gonzalez CF, Keyhan M, Blake R 2nd, and Matin A. Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction. Environ Microbiol 6: 851-860, 2004. (Pubitemid 39017268)
    • (2004) Environmental Microbiology , vol.6 , Issue.8 , pp. 851-860
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  • 2
    • 66149133646 scopus 로고    scopus 로고
    • Interrogating the molecular details of the peroxiredoxin activity of the Escherichia coli bacterioferritin comigratory protein using high-resolution mass spectrometry
    • Clarke DJ, Mackay CL, Campopiano DJ, Langridge-Smith P, and Brown AR. Interrogating the molecular details of the peroxiredoxin activity of the Escherichia coli bacterioferritin comigratory protein using high-resolution mass spectrometry. Biochemistry 48: 3904-3914, 2009.
    • (2009) Biochemistry , vol.48 , pp. 3904-3914
    • Clarke, D.J.1    MacKay, C.L.2    Campopiano, D.J.3    Langridge-Smith, P.4    Brown, A.R.5
  • 4
    • 79958059617 scopus 로고    scopus 로고
    • Structurebased insights into the catalytic power and conformational dexterity of peroxiredoxins
    • Hall A, Nelson K, Poole LB, and Karplus PA. Structurebased insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxid Redox Signal 15: 795-815, 2011.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 795-815
    • Hall, A.1    Nelson, K.2    Poole, L.B.3    Karplus, P.A.4
  • 5
    • 80054771975 scopus 로고    scopus 로고
    • Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin
    • Reeves SA, Parsonage D, Nelson KJ, and Poole LB. Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin. Biochemistry 50: 8970-8981, 2011.
    • (2011) Biochemistry , vol.50 , pp. 8970-8981
    • Reeves, S.A.1    Parsonage, D.2    Nelson, K.J.3    Poole, L.B.4
  • 6
    • 0037065722 scopus 로고    scopus 로고
    • An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum
    • DOI 10.1021/bi011802p
    • Reynolds CM, Meyer J, and Poole LB. An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum. Biochemistry 41: 1990-2001, 2002. (Pubitemid 34132274)
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1990-2001
    • Reynolds, C.M.1    Meyer, J.2    Poole, L.B.3
  • 8
    • 18844398674 scopus 로고    scopus 로고
    • The plant multigenic family of thiol peroxidases
    • DOI 10.1016/j.freeradbiomed.2004.07.037, PII S0891584904006331
    • Rouhier N and Jacquot JP. The plant multigenic family of thiol peroxidases. Free Radic Biol Med 38: 1413-1421, 2005. (Pubitemid 40693826)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.11 , pp. 1413-1421
    • Rouhier, N.1    Jacquot, J.-P.2
  • 9
    • 77749288943 scopus 로고    scopus 로고
    • Characterization of a thioredoxinthioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima
    • Yang X and Ma K. Characterization of a thioredoxinthioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol 192: 1370-1376, 2010.
    • (2010) J Bacteriol , vol.192 , pp. 1370-1376
    • Yang, X.1    Ma, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.