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Angewandte Chemie International Edition in English
Volumn 32, Issue 7, 1993, Pages 1062-1065
How N2 Might Be Activated by the FeMo‐Cofactor in Nitrogenase
Author keywords

[No Author keywords available]
Indexed keywords

EID: 33750497852     PISSN: 05700833     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.199310621     Document Type: Article
Times cited : (136)
References (23)
  • 3
    • 0002345759 scopus 로고
    • Röntgenstrukturanalyse von FeMo-Nitrogenase der enzymatischen ist das Problem der enzymatischen N2-Fixierung gelöst?
    • 67
    • (1993) Angewandte Chemie , vol.105
    • Sellman, D.1
  • 5
    • 0027159222 scopus 로고
    • A 2.2 Å resolution refinement has just been published:,. There are no major changes in the model
    • (1993) Science , vol.260 , pp. 792-794
    • Chan, M.K.1    Kim, J.2    Rees, D.C.3
  • 10
    • 84989565179 scopus 로고    scopus 로고
    • We also performed calculations on the cofactor model with real ligating atoms and the geometry from the X‐ray crystallographic analysis, and obtained similar results.
  • 19
    • 84989553086 scopus 로고    scopus 로고
    • 2 binding are not affected.
  • 20
    • 84989529649 scopus 로고    scopus 로고
    • 2(OP = 0.07). In addition there is reasonable Fe‐O bonding.
  • 21
    • 84989553079 scopus 로고    scopus 로고
    • 2‐Binding studies with two protons bound to two bridging sulfide ions, and to Fe2 and Fe5 along the perpendicular direction of the coordination planes, respectively.
  • 23
    • 84989553090 scopus 로고    scopus 로고
    • 2− raises the energy of the HOMO by 0.4 eV. Of course, 10 is impossible in this case.

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.