337 related articles for article (PubMed ID: 12206666)
1. Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin.
McCarthy AA; Walsh MA; Verma CS; O'Connell DP; Reinhold M; Yalloway GN; D'Arcy D; Higgins TM; Voordouw G; Mayhew SG
Biochemistry; 2002 Sep; 41(36):10950-62. PubMed ID: 12206666
[TBL] [Abstract][Full Text] [Related]
2. Evaluation of the electrostatic effect of the 5'-phosphate of the flavin mononucleotide cofactor on the oxidation--reduction potentials of the flavodoxin from desulfovibrio vulgaris (Hildenborough).
Zhou Z; Swenson RP
Biochemistry; 1996 Sep; 35(38):12443-54. PubMed ID: 8823179
[TBL] [Abstract][Full Text] [Related]
3. 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.
Swenson RP; Krey GD
Biochemistry; 1994 Jul; 33(28):8505-14. PubMed ID: 8031784
[TBL] [Abstract][Full Text] [Related]
4. Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentials.
Hoover DM; Drennan CL; Metzger AL; Osborne C; Weber CH; Pattridge KA; Ludwig ML
J Mol Biol; 1999 Dec; 294(3):725-43. PubMed ID: 10610792
[TBL] [Abstract][Full Text] [Related]
5. Modulation of the redox potentials of FMN in Desulfovibrio vulgaris flavodoxin: thermodynamic properties and crystal structures of glycine-61 mutants.
O'Farrell PA; Walsh MA; McCarthy AA; Higgins TM; Voordouw G; Mayhew SG
Biochemistry; 1998 Jun; 37(23):8405-16. PubMed ID: 9622492
[TBL] [Abstract][Full Text] [Related]
6. Role of glutamate-59 hydrogen bonded to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin. Glutamate-59 is not responsible for the pH dependency but contributes to the stabilization of the flavin semiquinone.
Bradley LH; Swenson RP
Biochemistry; 1999 Sep; 38(38):12377-86. PubMed ID: 10493805
[TBL] [Abstract][Full Text] [Related]
7. Role of hydrogen bonding interactions to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin.
Bradley LH; Swenson RP
Biochemistry; 2001 Jul; 40(30):8686-95. PubMed ID: 11467928
[TBL] [Abstract][Full Text] [Related]
8. Electrostatic effects of surface acidic amino acid residues on the oxidation-reduction potentials of the flavodoxin from Desulfovibrio vulgaris (Hildenborough).
Zhou Z; Swenson RP
Biochemistry; 1995 Mar; 34(10):3183-92. PubMed ID: 7880813
[TBL] [Abstract][Full Text] [Related]
9. X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) apoflavodoxin-riboflavin complex.
Walsh MA; McCarthy A; O'Farrell PA; McArdle P; Cunningham PD; Mayhew SG; Higgins TM
Eur J Biochem; 1998 Dec; 258(2):362-71. PubMed ID: 9874201
[TBL] [Abstract][Full Text] [Related]
10. pH-dependent spectroscopic changes associated with the hydroquinone of FMN in flavodoxins.
Yalloway GN; Mayhew SG; Malthouse JP; Gallagher ME; Curley GP
Biochemistry; 1999 Mar; 38(12):3753-62. PubMed ID: 10090764
[TBL] [Abstract][Full Text] [Related]
11. The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris [Hildenborough].
Zhou Z; Swenson RP
Biochemistry; 1996 Dec; 35(50):15980-8. PubMed ID: 8973168
[TBL] [Abstract][Full Text] [Related]
12. The midpoint potentials for the oxidized-semiquinone couple for Gly57 mutants of the Clostridium beijerinckii flavodoxin correlate with changes in the hydrogen-bonding interaction with the proton on N(5) of the reduced flavin mononucleotide cofactor as measured by NMR chemical shift temperature dependencies.
Chang FC; Swenson RP
Biochemistry; 1999 Jun; 38(22):7168-76. PubMed ID: 10353827
[TBL] [Abstract][Full Text] [Related]
13. Structures and comparison of the Y98H (2.0 A) and Y98W (1.5 A) mutants of flavodoxin (Desulfovibrio vulgaris).
Reynolds RA; Watt W; Watenpaugh KD
Acta Crystallogr D Biol Crystallogr; 2001 Apr; 57(Pt 4):527-35. PubMed ID: 11264581
[TBL] [Abstract][Full Text] [Related]
14. Role of methionine 56 in the control of the oxidation-reduction potentials of the Clostridium beijerinckii flavodoxin: effects of substitutions by aliphatic amino acids and evidence for a role of sulfur-flavin interactions.
Druhan LJ; Swenson RP
Biochemistry; 1998 Jul; 37(27):9668-78. PubMed ID: 9657679
[TBL] [Abstract][Full Text] [Related]
15. Structural changes caused by site-directed mutagenesis of tyrosine-98 in Desulfovibrio vulgaris flavodoxin delineated by 1H and 15N NMR spectroscopy: implications for redox potential modulation.
Stockman BJ; Richardson TE; Swenson RP
Biochemistry; 1994 Dec; 33(51):15298-308. PubMed ID: 7803393
[TBL] [Abstract][Full Text] [Related]
16. Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes.
Ludwig ML; Pattridge KA; Metzger AL; Dixon MM; Eren M; Feng Y; Swenson RP
Biochemistry; 1997 Feb; 36(6):1259-80. PubMed ID: 9063874
[TBL] [Abstract][Full Text] [Related]
17. Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 1. Kinetic evidence for cooperative effects associated with the binding of inorganic phosphate and the 5'-phosphate moiety of the cofactor.
Murray TA; Swenson RP
Biochemistry; 2003 Mar; 42(8):2307-16. PubMed ID: 12600198
[TBL] [Abstract][Full Text] [Related]
18. Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials.
Lostao A; Gómez-Moreno C; Mayhew SG; Sancho J
Biochemistry; 1997 Nov; 36(47):14334-44. PubMed ID: 9398151
[TBL] [Abstract][Full Text] [Related]
19. Alanine-scanning of the 50's loop in the Clostridium beijerinckii flavodoxin: evaluation of additivity and the importance of interactions provided by the main chain in the modulation of the oxidation-reduction potentials.
Kasim M; Swenson RP
Biochemistry; 2001 Nov; 40(45):13548-55. PubMed ID: 11695902
[TBL] [Abstract][Full Text] [Related]
20. Regulation of oxidation-reduction potentials through redox-linked ionization in the Y98H mutant of the Desulfovibrio vulgaris [Hildenborough] flavodoxin: direct proton nuclear magnetic resonance spectroscopic evidence for the redox-dependent shift in the pKa of Histidine-98.
Chang FC; Swenson RP
Biochemistry; 1997 Jul; 36(29):9013-21. PubMed ID: 9220989
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
