Vinayaka, CR and Rao, VSR (1987) A computer modelling approach to study the mode of binding of L-lyxoflavin-5'-monophosphate to flavodoxin. In: Journal of Biomolecular Structure & Dynamics, 4 (6). pp. 1095-1103.Full text not available from this repository. (Request a copy)
The mode of binding of L-lyxoflavin-5'-monophosphate was studied by a computer modeling method. Energetically preferred conformers fo L-lyxoflavin-5'-monophosphate were obtained using empirical potential energy functions. These min. energy conformers were used to study the mode of their binding to flavodoxin. The study indicates that L-lyxoflavin-5'-monophosphate can also have coenzymic activity similar to FMN. However, its lower activity compared to FMN is due to the lower conformer population that initiates the binding process. Also, the inability of L-lyxoflavin to promote growth in some cases appears to be at the phosphorylation level and not at the coenzyme level.
|Item Type:||Journal Article|
|Additional Information:||Copyright belongs to Adenine Press|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||25 Mar 2008|
|Last Modified:||27 Aug 2008 13:16|
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