Designing molecules for PDT: red light-induced DNA cleavage on disulfide bond activation in a dicopper(ii) complex

2005 ◽  
pp. 344 ◽  
Author(s):  
Shanta Dhar ◽  
Munirathinam Nethaji ◽  
Akhil R. Chakravarty
Keyword(s):  
Disulfide Bond ◽  
Dna Cleavage ◽  
Bond Activation ◽  
Red Light

scholarly journals Anaerobic DNA cleavage in red light by dicopper(II) complexes on disulphide bond activation

2010 ◽  
Vol 122 (3) ◽  
pp. 321-333 ◽  
Author(s):  
Debojyoti Lahiri ◽  
Ritankar Majumdar ◽  
Ashis K. Patra ◽  
Akhil R. Chakravarty
Keyword(s):  
Dna Cleavage ◽  
Bond Activation ◽  
Red Light ◽  
Disulphide Bond

scholarly journals Correction to Copper(II) Complexes of l-Arginine as Netropsin Mimics Showing DNA Cleavage Activity in Red Light

2019 ◽  
Vol 58 (19) ◽  
pp. 13502-13503
Author(s):  
Ashis K. Patra ◽  
Tuhin Bhowmick ◽  
Sovan Roy ◽  
Suryanarayanarao Ramakumar ◽  
Akhil R. Chakravarty
Keyword(s):  
Dna Cleavage ◽  
Red Light ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

scholarly journals Correction to Metal-Based Netropsin Mimics Showing AT-Selective DNA Binding and DNA Cleavage Activity at Red Light

2019 ◽  
Vol 58 (14) ◽  
pp. 9514-9514
Author(s):  
Ashis K. Patra ◽  
Tuhin Bhowmick ◽  
Suryanarayanarao Ramakumar ◽  
Akhil R. Chakravarty
Keyword(s):  
Dna Binding ◽  
Dna Cleavage ◽  
Red Light ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Selective Dna Binding

Anaerobic DNA cleavage activity in red light and photocytotoxicity of (pyridine-2-thiol)cobalt(iii) complexes of phenanthroline bases

2010 ◽  
Vol 39 (7) ◽  
pp. 1807 ◽  
Author(s):  
Debojyoti Lahiri ◽  
Sovan Roy ◽  
Sounik Saha ◽  
Ritankar Majumdar ◽  
Rajan R. Dighe ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Red Light ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Phenanthroline Bases

Metal-Based Netropsin Mimics Showing AT-Selective DNA Binding and DNA Cleavage Activity at Red Light

2007 ◽  
Vol 46 (22) ◽  
pp. 9030-9032 ◽  
Author(s):  
Ashis K. Patra ◽  
Tuhin Bhowmick ◽  
Suryanarayanarao Ramakumar ◽  
Akhil R. Chakravarty
Keyword(s):  
Dna Binding ◽  
Dna Cleavage ◽  
Red Light ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Selective Dna Binding

scholarly journals Metal-assisted red light-induced DNA cleavage by ternary l-methionine copper(ii) complexes of planar heterocyclic bases

2005 ◽  
pp. 896 ◽  
Author(s):  
Ashis K. Patra ◽  
Shanta Dhar ◽  
Munirathinam Nethaji ◽  
Akhil R. Chakravarty
Keyword(s):  
Dna Cleavage ◽  
Red Light ◽  
Heterocyclic Bases

Chlorin-Oligonucleotide Conjugates:  Synthesis, Properties, and Red Light-Induced Photochemical Sequence-Specific DNA Cleavage in Duplexes and Triplexes†,‡

1996 ◽  
Vol 118 (40) ◽  
pp. 9469-9476 ◽  
Author(s):  
Alexandre S. Boutorine ◽  
Daniel Brault ◽  
Masashi Takasugi ◽  
Olavio Delgado ◽  
Claude Hélène
Keyword(s):  
Dna Cleavage ◽  
Red Light ◽  
Synthesis Properties ◽  
Oligonucleotide Conjugates

scholarly journals Regulation of a Phage Endolysin by Disulfide Caging

2010 ◽  
Vol 192 (21) ◽  
pp. 5682-5687 ◽  
Author(s):  
Gabriel F. Kuty ◽  
Min Xu ◽  
Douglas K. Struck ◽  
Elizabeth J. Summer ◽  
Ry Young
Keyword(s):  
Cell Wall ◽  
Disulfide Bond ◽  
Active Site ◽  
Bond Activation ◽  
Inactive Form ◽  
Signal Anchor ◽  
Disulfide Bond Isomerization ◽  
Disulfide Isomerization ◽  
Wall Signal ◽  
Gain Access

ABSTRACT In contrast to canonical phage endolysins, which require holin-mediated disruption of the membrane to gain access to attack the cell wall, signal anchor release (SAR) endolysins are secreted by the host sec system, where they accumulate in an inactive form tethered to the membrane by their N-terminal SAR domains. SAR endolysins become activated by various mechanisms upon release from the membrane. In its inactive form, the prototype SAR endolysin, LyzP1, of coliphage P1, has an active-site Cys covalently blocked by a disulfide bond; activation involves a disulfide bond isomerization driven by a thiol in the newly released SAR domain, unblocking the active-site Cys. Here, we report that Lyz103, the endolysin of Erwinia phage ERA103, is also a SAR endolysin. Although Lyz103 does not have a catalytic Cys, genetic evidence suggests that it also is activated by a thiol-disulfide isomerization triggered by a thiol in the SAR domain. In this case, the inhibitory disulfide in nascent Lyz103 is formed between cysteine residues flanking a catalytic glutamate, caging the active site. Thus, LyzP1 and Lyz103 define subclasses of SAR endolysins that differ in the nature of their inhibitory disulfide, and Lyz103 is the first enzyme found to be regulated by disulfide bond caging of its active site.

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