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Volumn 118, Issue 5, 1996, Pages 1113-1117

X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE;

EID: 0029926237     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja953317l     Document Type: Article
Times cited : (128)

References (47)
  • 20
    • 13344258355 scopus 로고    scopus 로고
    • note
    • The EXAFSPAK program suite was developed by one of the authors (G.N.G.) and is available by application in writing to the authors.
  • 24
    • 49649145902 scopus 로고
    • Double integration of EPR spectra was performed using a 1 mM CuEDTA standard with correction for transition probability [Aasa, R.; Vånngård. T. J. Magn. Reson. 1975, 19, 308-315].
    • (1975) J. Magn. Reson. , vol.19 , pp. 308-315
    • Aasa, R.1    Vånngård, T.2
  • 31
    • 0000720440 scopus 로고
    • Long 2.9 Å Cu-S(methionine) EXAFS has previously proved impossible to detect in plastocyanin, even when using polarized single crystal EXAFS to provide the most favorable conditions for detection. See: Penner-Hahn, J. E.; Murata, M.: Hodgson, K. Ï.; Freeman. H. Inorg. Chem. 1989, 28, 1826-1832.
    • (1989) Inorg. Chem. , vol.28 , pp. 1826-1832
    • Penner-Hahn, J.E.1    Murata, M.2    Hodgson, K.Ï.3    Freeman, H.4
  • 33
    • 13344296562 scopus 로고    scopus 로고
    • note
    • 31, and assuming that the non-sulfur ligands are oxygens (rather than nitrogen).
  • 37
    • 0024506359 scopus 로고
    • George, G. N.; Turner, N. A.; Bray, R. C.; Morpeth, F. F.; Boxer, D. H.; Cramer, S. P. Biochem. J. 1989, 259, 693-700. Note that an earlier study on enzyme prepared using a different purifation method gave quite different EXAFS results [Cramer, S. P.; Solmonson, L. P.; Adams, M. W. W.; Mortenson, L. E. J. Am. Chem. Soc. 1984, 106, 1467-1471]. The earlier study reported long-distance interactions to an unknown scatterer at about 2.7 Å, and it seems likely that the active site can adopt at least two different structures.
    • (1989) Biochem. J. , vol.259 , pp. 693-700
    • George, G.N.1    Turner, N.A.2    Bray, R.C.3    Morpeth, F.F.4    Boxer, D.H.5    Cramer, S.P.6
  • 38
    • 0001380448 scopus 로고
    • George, G. N.; Turner, N. A.; Bray, R. C.; Morpeth, F. F.; Boxer, D. H.; Cramer, S. P. Biochem. J. 1989, 259, 693-700. Note that an earlier study on enzyme prepared using a different purifation method gave quite different EXAFS results [Cramer, S. P.; Solmonson, L. P.; Adams, M. W. W.; Mortenson, L. E. J. Am. Chem. Soc. 1984, 106, 1467-1471]. The earlier study reported long-distance interactions to an unknown scatterer at about 2.7 Å, and it seems likely that the active site can adopt at least two different structures.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 1467-1471
    • Cramer, S.P.1    Solmonson, L.P.2    Adams, M.W.W.3    Mortenson, L.E.4
  • 47
    • 0023655717 scopus 로고
    • While molybdenum cis di-oxo enzymes such as sulfite oxidase may indeed function by oxo transfer, there is some doubt about the molybdenum hydroxylases such as xanthine oxidase which contain molybdenum oxothiolato active sites. For these enzymes such a mechanism would involve breaking of the strong Mo=O bond, and destabilization of this by Mo=S (as opposed to another Mo=O) is likely to be subtle at best. While concrete evidence does exist for catalytic oxygen exchange with a solvent-exchangeable water in xanthine oxidase [see: Hille, R.: Sprecher, H. J. Biol. Chem. 1987, 262, 10914-10917]; however, direct evidence for a Mo=O transfer mechanism in the molybdenum hydroxylases is lacking.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10914-10917
    • Hille, R.1    Sprecher, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.