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Volumn 125, Issue 48, 2003, Pages 14696-14697

Intramolecular Electron Transfer in a Bacterial Sulfite Dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HEME; IRON; MOLYBDENUM; RECOMBINANT ENZYME; SULFATE; SULFITE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0345724820     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja038197t     Document Type: Article
Times cited : (21)

References (19)
  • 2
    • 0036359683 scopus 로고    scopus 로고
    • Molybdenum and Tungsten: Their Roles in Biological Processes: Sigel, A., Sigel, H., Ed.; Marcel Dekker: NY
    • Enemark, J. H., Cosper, M. M. In Metal Ions in Biological Systems; Molybdenum and Tungsten: Their Roles in Biological Processes, Vol. 39: Sigel, A., Sigel, H., Ed.; Marcel Dekker: NY, 2002; pp 621-654.
    • (2002) Metal Ions in Biological Systems , vol.39 , pp. 621-654
    • Enemark, J.H.1    Cosper, M.M.2
  • 16
    • 84955331315 scopus 로고    scopus 로고
    • Balzani, V., Ed.; Wiley-VCH: Weinheim
    • Tollin, G. In Electron Transfer in Chemistry; Balzani, V., Ed.; Wiley-VCH: Weinheim, 2001; Vol. IV, pp 202-231.
    • (2001) Electron Transfer in Chemistry , vol.4 , pp. 202-231
    • Tollin, G.1
  • 17
    • 0344544668 scopus 로고    scopus 로고
    • note
    • The peak wavelengths (553 and 523 nm) observed in the flash-induced difference spectra are identical to those observed in the steady-state difference spectrum for heme reduction. These spectra confirm that the transient absorbance changes observed at 553 nm are directly related to reduction and reoxidation of the c-type heme prosthetic group. No detectable spectral contribution from the Mo cofactor was observed.
  • 19
    • 0344113007 scopus 로고    scopus 로고
    • note
    • Steady-state kinetics were conducted in 20 mM Bis-Tris buffer (pH 6.0), with a saturated concentration of horse heart cytochrome c (40 μM).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.