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Volumn 120, Issue 32, 1998, Pages 8102-8112

Synthesis, structures, and oxo transfer reactivity of bis(dithiolene)tungsten(IV,VI) complexes related to the active sites of tungstoenzymes

Author keywords

[No Author keywords available]

Indexed keywords

BIS(DITHIOLENE)TUNGSTEN COMPLEX; METAL COMPLEX; METALLOPROTEIN; OXIDOREDUCTASE; TUNGSTEN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0032547302     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja981015o     Document Type: Article
Times cited : (124)

References (89)
  • 11
    • 0030592449 scopus 로고    scopus 로고
    • Independent crystal structures of Rhodobacter capsulatus DMSO reductase do not give the same Mo site structures nor do they agree with that found in the R. sphaeroides enzyme: (a) Schneider, F.; Löwe, J.; Huber, R.; Schindelin, H.; Kisker, C.; Knäblein, J. J. Mol. Biol. 1996, 263, 53. (b) McAlpine, A. S.; McEwan, A. G.; Shaw, A. L.; Bailey, S. JBIC 1997, 2, 690. See also: (c) McAlpine, A. S.; McEwan, A. G.; Bailey, S. J. Mol. Biol. 1998, 275, 613. Because the origin of these discrepancies is not clear, we display the sites of the R. sphaeroides enzyme in Figure 1; these bear a closer relationship to the tungsten coordination units prepared in this investigation.
    • (1996) J. Mol. Biol. , vol.263 , pp. 53
    • Schneider, F.1    Löwe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knäblein, J.6
  • 12
    • 0031444936 scopus 로고    scopus 로고
    • Independent crystal structures of Rhodobacter capsulatus DMSO reductase do not give the same Mo site structures nor do they agree with that found in the R. sphaeroides enzyme: (a) Schneider, F.; Löwe, J.; Huber, R.; Schindelin, H.; Kisker, C.; Knäblein, J. J. Mol. Biol. 1996, 263, 53. (b) McAlpine, A. S.; McEwan, A. G.; Shaw, A. L.; Bailey, S. JBIC 1997, 2, 690. See also: (c) McAlpine, A. S.; McEwan, A. G.; Bailey, S. J. Mol. Biol. 1998, 275, 613. Because the origin of these discrepancies is not clear, we display the sites of the R. sphaeroides enzyme in Figure 1; these bear a closer relationship to the tungsten coordination units prepared in this investigation.
    • (1997) JBIC , vol.2 , pp. 690
    • McAlpine, A.S.1    McEwan, A.G.2    Shaw, A.L.3    Bailey, S.4
  • 13
    • 0032579202 scopus 로고    scopus 로고
    • Independent crystal structures of Rhodobacter capsulatus DMSO reductase do not give the same Mo site structures nor do they agree with that found in the R. sphaeroides enzyme: (a) Schneider, F.; Löwe, J.; Huber, R.; Schindelin, H.; Kisker, C.; Knäblein, J. J. Mol. Biol. 1996, 263, 53. (b) McAlpine, A. S.; McEwan, A. G.; Shaw, A. L.; Bailey, S. JBIC 1997, 2, 690. See also: (c) McAlpine, A. S.; McEwan, A. G.; Bailey, S. J. Mol. Biol. 1998, 275, 613. Because the origin of these discrepancies is not clear, we display the sites of the R. sphaeroides enzyme in Figure 1; these bear a closer relationship to the tungsten coordination units prepared in this investigation.
    • (1998) J. Mol. Biol. , vol.275 , pp. 613
    • McAlpine, A.S.1    McEwan, A.G.2    Bailey, S.3
  • 42
    • 3543021629 scopus 로고
    • Wiley: New York
    • (b) Ferretti, A. Organic Syntheses, Wiley: New York, 1973; Collect. Vol. V, p 419.
    • (1973) Organic Syntheses , vol.5 COLLECT. VOL , pp. 419
    • Ferretti, A.1
  • 47
    • 3543021630 scopus 로고    scopus 로고
    • note
    • See paragraph at the end of this article concerning Supporting Information available.
  • 51
    • 3543037699 scopus 로고    scopus 로고
    • note
    • t in the reaction system is unclear, but 6 is not formed in its absence.
  • 62
    • 3543007850 scopus 로고    scopus 로고
    • note
    • 36a
  • 79
    • 0001230482 scopus 로고
    • 2 conversion with the same reagent, cf: Yu, S.-B.; Holm, R. H. Inorg. Chem. 1989, 28, 4385.
    • (1989) Inorg. Chem. , vol.28 , pp. 4385
    • Yu, S.-B.1    Holm, R.H.2
  • 80
    • 3543043891 scopus 로고    scopus 로고
    • note
    • V-OH species. The latter itself, or by bimolecular condensation to form water, could supply the protons necessary for decoordination of bdt, which can function as a ligand and as a reductant when bound or free. Use of NaOMe led to a mixture of 2 and 7, again requiring a reductive pathway.
  • 81
    • 3543018034 scopus 로고    scopus 로고
    • note
    • 3CN): δ 6.90 (4, dd), 7.12 (1, t), 7.32 (2. d), 7.40 (4, dd), 7.75 (2, d).
  • 82
    • 3543044499 scopus 로고    scopus 로고
    • note
    • 20


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.