Novel cofactor derivatives and cofactor-based models
References (31)
- et al.
Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogues to serve as substrates in vitro for E. coli holo-ACP synthase
Chem Biol
(1997) - et al.
How coenzyme B12 radicals are generated: the crystal structure of methylmalonylcoenzyme A mutase a 2 Å resolution
Structure
(1996) - et al.
Determination of the gene sequence and the three-dimensional structure at 2.4 Å resolution of methanol dehydrogenase from Methylophilus W3A1
J Mol Biol
(1996) - et al.
The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å
Structure
(1995) - et al.
Active-site probes of flavoproteins
Biochem Soc Trans
(1980) - et al.
A theoretical study of the structures of flavin in different oxidation and protonation states
J Am Chem Soc
(1996) - et al.
Conformational effects on flavin redox chemistry
J Org Chem
(1997) - et al.
Linear free energy substituent effect on flavin redox chemistry (of special interest)
J Am Chem Soc
(1998) - et al.
Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions
Biochemistry
(1994) - et al.
Model systems for flavoenzyme activity. Modulation of flavin redox potentials through -stacking interactions (of outstanding interest)
J Am Chem Soc
(1997)
Model systems for flavoenzyme activity: one- and two-electron reduction of flavins in aprotic hydrophobic environments (of special interest)
J Am Chem Soc
(1997)
Model systems for flavoenzyme activity. Stabilization of the Flavin Radical anion through specific hydrogen bond interactions
J Am Chem Soc
(1995)
Electrochemical control of recognition processes. A three-component molecular switch
J Am Chem Soc
(1997)
Model systems for flavoenzyme activity. Specific hydrogen bond recognition of flavin in a silicate sol-gel
J Am Chem Soc
(1997)
Application of a nitrospiropyran-FAD-reconstituted glucose oxidase and charged electron mediators as optobioelectronic assemblies for the amperometric transduction of recorded optical signals: control of the ‘on’-‘off’ direction of the photoswitch
J Am Chem Soc
(1997)
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