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Volumn 9, Issue 1, 2003, Pages 76-87

Electron-transfer chemistry of the iron-molybdenum cofactor of nitrogenase: Delocalized and localized reduced states of FeMoco which allow binding of carbon monoxide to iron and molybdenum

Author keywords

Bridging ligands; Cofactors; Electrochemistry; IR spectroscopy; Nitrogen fixation; Nitrogenases

Indexed keywords

CARBON MONOXIDE; ENZYMES; IRON COMPOUNDS; ISOMERIZATION;

EID: 0346034548     PISSN: 09476539     EISSN: None     Source Type: Journal    
DOI: 10.1002/chem.200390033     Document Type: Article
Times cited : (43)

References (48)
  • 33
    • 0034790714 scopus 로고    scopus 로고
    • We thank a referee for drawing attention to the possibility that the redox interconversion might be a consequence of oligomerisation. [P. Frank, H. C. Angove, B. K. Burgess, K. O. Hodgson, J. Biol. Inorg. Chem. 2001, 6, 683-697.] However, the cyclic voltammetric response of the native cofactor as typified by Figure 3a fits well to a simulated scheme of squares for a one-electron redox-linked interconversion between isomeric forms, A similar voltammetric response can be simulated for monomer - dimer (first peak/second peak) redox-linked interconversion, but critically conversion to a single monomeric thiophenolate form is predicted to give a 35% increase in the primary peak current for the isomerism and a 60% increase for a monomerdimer interconversion. Experimentally we find a 31% increase, which is consistent with the former. Similar arguments obtain for higher "oligomeric" forms.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 683-697
    • Frank, P.1    Angove, H.C.2    Burgess, B.K.3    Hodgson, K.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.