| Name | thioredoxin reductase |
|---|---|
| Synonyms | ACR 1; PLP; ACR1; AOEB166; Alu corepressor 1; Antioxidant enzyme B166; B166; Liver tissue 2D page spot 71B… |
| Name | azobenzene |
|---|---|
| CAS | diphenyldiazene |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 10984402 | Renner C, Cramer J, Behrendt R, Moroder L: Photomodulation of conformational states. Biopolymers. 2000 Dec;54(7):501-14. Correspondingly, the active-site octapeptide fragment H--Cys---Cys-Asp-Gly--OH [134-141] of thioredoxin reductase, with its high preference for a 3 (10)-helix turn conformation centered on the -Cys sequence, was backbone cyclized with this azobenzene moiety in the attempt to design a photoresponsive system where the conformational states of the peptide backbone are dictated by the configuration of the azobenzene and can be further modulated by the disulfide bridge. |
31(0,1,1,1) | Details |
| 10984401 | Renner C, Behrendt R, Sporlein S, Wachtveitl J, Moroder L: Photomodulation of conformational states. Biopolymers. 2000 Dec;54(7):489-500. The thioredoxin reductase active-site fragment H--Cys---Cys-Asp-Gly--OH [134-141], which is known for its high tendency to assume an almost identical conformation as in the intact enzyme, was backbone cyclized with the photoresponsive (4-amino) phenylazobenzoic acid (APB) to produce a monocyclic and disulfide-bridged bicyclic APB-peptide. First femtosecond spectroscopic analysis of the dynamics of the photoreaction confirm a fast first phase on the femtosecond time scale related to the cis/trans isomerization of the azobenzene moiety followed by a slower phase in the picosecond time scale that involves an adjustment of the peptide backbone. |
1(0,0,0,1) | Details |
| 11920439 | Renner C, Behrendt R, Heim N, Moroder L: Photomodulation of conformational states. Biopolymers. 2002 May;63(6):382-93. In previous studies we have shown that light-induced cis/trans isomerization of the azobenzene moiety in cyclo--Cys---Cys-Asp-Gly--AMPB] [AMPB: (4-aminomethyl) phenylazobenzoic acid] leads both in the monocyclic and in the oxidized bicyclic form to markedly differentiated conformational states in DMSO, a fact that lends itself for photomodulation of the redox potential of such bis-cysteinyl-peptides. For this purpose water-soluble systems are required, and this was achieved by replacing three residues outside the Cys---Cys active-site motif of thioredoxin reductase with lysines. |
1(0,0,0,1) | Details |
| 15637699 | Milbradt AG, Loweneck M, Krupka SS, Reif M, Sinner EK, Moroder L, Renner C: Photomodulation of conformational states. Biopolymers. 2005 Apr 5;77(5):304-13. In previous studies we have investigated octapeptides backbone-cyclized by (4-amino) phenyl azobenzoic acid (APB) or (4-aminomethyl) phenylazobenzoic acid (AMPB) and containing the active-site sequence Cys---Cys-Asp from the thioredoxin reductase. The conformational and redox properties of these peptides were strongly dependent on the isomeric state of the azobenzene chromophore. |
1(0,0,0,1) | Details |