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  • 1
    Electronic Resource
    Electronic Resource
    A MINDO/3 MO study of oxidized flavins (1981)
    Springer
    Theoretical chemistry accounts 60 (1981), S. 127-141 
    Details
    ISSN: 1432-2234
    Keywords: Flavins ; Isoalloxazines ; MINDO/3 ; NMR ; Energies ; Dipole moments ; Ionization potentials ; Electron affinities ; Semiempirical
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The use of semi-empirical molecular orbital methods for the study of biologically important molecules has increased in recent years. The validity of well-known approximate Hartree-Fock molecular orbital methods such as MINDO/3 and MNDO still remains largely untested for biological molecules. Here we report its first application to the study of the electronic structures of isoalloxazines. Electronic charge distribution, variation of dipole moment, first ionization potential, electron affinity, orbital energies and electronic transitions are examined. Some of these results are compared with experiments. Good correlations with experiments were generally found in net atomic charge distributions, ionization potentials and electronic transitions. As a result of relatively good correlations with experiment application of the MINDO/3 method for extended study of biologically important coenzymes is promising.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00550331
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    MO Study of flavin-protein interactions in flavodoxin catalysis (1980)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 18 (1980), S. 449-456 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: MINDO/3 calculations have been performed on the Clostridium MP flavodoxin active site (a complex of the redox active coenzyme flavin mononucleotide sandwiched between the side chains of methionine and tryptophan) at various redox levels using coordinates derived from x-ray diffraction studies of the holoenzyme. Frontier orbital indices were calculated and indicate that reduction of the flavin is accompanied by induced polar states in the amino acid side chains. This stabilization of charge by the amino acid side chains could account for the reaction rate enhancement of flavin reduction catalyzed by flavodoxin. Frontier orbitals for free flavin, for the flavodoxin bound flavin without the amino acid side chains, and for the oxidized Desulfovibrio vulgaris flavodoxin active site were computed for comparison.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560180214
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    MO study of flavin reduction (1982)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 22 (1982), S. 583-594 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: MINDO/3 calculations have been performed on semiquinone and fully reduced lumiflavins and on hydroperoxy adducts of lumiflavin. Frontier orbital indices were calculated. Reduction of the flavin was studied in bent and planar flavin rings. The results suggest that the planar reduced flavin has a smaller ionization potential than the bent reduced flavin. This could account for the low redox potential of protein-bound reduced flavins.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560220310
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    Paper (German National Licenses)
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