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Volumn 122, Issue 14, 2000, Pages 3517-3521

Model systems for flavoenzyme activity. The role of N(3)-H hydrogen bonding in flavin redox processes

Author keywords

[No Author keywords available]

Indexed keywords

FLAVOPROTEIN; LUMIFLAVINE;

EID: 0034639898     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja994204v     Document Type: Article
Times cited : (65)

References (53)
  • 1
    • 0004255912 scopus 로고
    • Müller, F., Ed.; CRC: Boca Raton
    • For an extensive review of flavin and flavoenzyme chemistry, see: Chemistry and Biochemistry of Flavoenzymes; Müller, F., Ed.; CRC: Boca Raton, 1991; Vols. 1-3.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.1-3
  • 18
    • 0000275732 scopus 로고    scopus 로고
    • For model studies of the role of conformational effects on flavin redox processes, see: Hasford, J.; Kemnitzer, W.; Rizzo, C. J. Org. Chem. 1997, 62, 5244-5245.
    • (1997) J. Org. Chem. , vol.62 , pp. 5244-5245
    • Hasford, J.1    Kemnitzer, W.2    Rizzo, C.3
  • 29
  • 32
    • 0030900924 scopus 로고    scopus 로고
    • For examples where N(3) alkyl flavins have been used to model flavoenzyme processes see: Hoegy, S.; Mariano, P. Tetrahedron 1997, 53, 5027-5046.
    • (1997) Tetrahedron , vol.53 , pp. 5027-5046
    • Hoegy, S.1    Mariano, P.2
  • 37
    • 0022837145 scopus 로고
    • For a previous computational study of the effects of hydrogen bonding on flavin LUMO energies, see: Nishimoto, K.; Fukunaga, H.; Yagi, K. J. Biochem. 1986, 100, 1647-1653.
    • (1986) J. Biochem. , vol.100 , pp. 1647-1653
    • Nishimoto, K.1    Fukunaga, H.2    Yagi, K.3
  • 47
    • 0031035026 scopus 로고    scopus 로고
    • Previous studies have shown that flavin 1 does not dimerize or aggregate at the concentrations used in this study: Breinlinger, E.; Rotello, V. J. Am. Chem. Soc. 1997, 119, 1165-1166.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1165-1166
    • Breinlinger, E.1    Rotello, V.2
  • 50
    • 33646331966 scopus 로고    scopus 로고
    • Since the comparison of reduction potentials between flavin 1 and 2 is calculated separately for each solvent system, any solvent effect experienced by the ferrocene is canceled out
    • Since the comparison of reduction potentials between flavin 1 and 2 is calculated separately for each solvent system, any solvent effect experienced by the ferrocene is canceled out.
  • 52
    • 33646307214 scopus 로고    scopus 로고
    • note
    • The change in reduction potential cannot be fully attributed to interruption of the hydrogen bond to N(3) due to indirect effects of the mutation along the protein backbone. The authors suggest that the mutated residue may function not only to provide a hydrogen bond to flavin at N(3) but also to constrain the protein backbone into a conformation that optimizes additional hydrogen bonds to the flavin cofactor at O(4) and N(5), complicating direct assignment of energetic contributions.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.