Title of article
The π–π* molecular structure of flavin of FADH− enzymatic cofactor using the LCAO method
Author/Authors
Hawke، نويسنده , , L.G.D. and Simserides، نويسنده , , C. and Kalosakas، نويسنده , , G.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2009
Pages
4
From page
266
To page
269
Abstract
The π–π* molecular structure (eigenenergies and eigenfunctions) of flavin tricyclic ring is calculated, using the linear combination of atomic orbitals (LCAO) method containing only pz atomic orbitals. In respect to FADH− position opposite to DNA lesion in photolyase, flavinʹs HOMO is found to be distributed in the central and distal side, while LUMO is localized in the distal side of flavin (the side that is closer to the adenine part of FADH− and farther than the DNA dimer lesion). LUMO1 as well as LUMO2 are mainly distributed in the proximal side of flavin (the side that is closer to the DNA dimer). Our findings are compared with previous theoretical results as well as with experimental values of known π–π* transitions.
Keywords
Organic substances , Electron states , Atoms and molecules
Journal title
MATERIALS SCIENCE & ENGINEERING: B
Serial Year
2009
Journal title
MATERIALS SCIENCE & ENGINEERING: B
Record number
2147203
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