Charge Redistribution in Oxidized and Semiquinone E. coli DNA Photolyase upon Photoexcitation: Stark Spectroscopy Reveals a Rationale for the Position of Trp382

2009 ◽  
Vol 131 (13) ◽  
pp. 4795-4807 ◽  
Author(s):  
Goutham Kodali ◽  
Salim U. Siddiqui ◽  
Robert J. Stanley
Keyword(s):  
Charge Redistribution ◽  
Stark Spectroscopy ◽  
Dna Photolyase ◽  
E Coli

scholarly journals Investigation of Excited State Charge Redistribution of the Reduced Anionic Flavin in DNA Photolyase and Simple Solvents by Stark Spectroscopy

2013 ◽  
Vol 104 (2) ◽  
pp. 488a
Author(s):  
Raymond F. Pauszek ◽  
Goutham Kodali ◽  
M. Salim Siddiqui ◽  
Kimberly Jacoby ◽  
Robert J. Stanley
Keyword(s):  
Excited State ◽  
Charge Redistribution ◽  
Stark Spectroscopy ◽  
Dna Photolyase ◽  
State Charge

Identification of oligothymidylates as new simple substrates for E. coli DNA photolyase and their use in a rapid spectrophotometric enzyme assay

Biochemistry ◽  
1985 ◽  
Vol 24 (8) ◽  
pp. 1856-1861 ◽  
Author(s):  
Marilyn Schuman Jorns ◽  
Gwendolyn B. Sancar ◽  
Aziz Sancar
Keyword(s):  
Enzyme Assay ◽  
Dna Photolyase ◽  
E Coli

Charge Transfer in E. coli DNA Photolyase: Understanding Polarization and Stabilization Effects via QM/MM Simulations

2013 ◽  
Vol 117 (37) ◽  
pp. 10769-10778 ◽  
Author(s):  
Gesa Lüdemann ◽  
P. Benjamin Woiczikowski ◽  
Tomáš Kubař ◽  
Marcus Elstner ◽  
Thomas B. Steinbrecher
Keyword(s):  
Charge Transfer ◽  
Dna Photolyase ◽  
E Coli

Activity assay of His-tagged E. coli DNA photolyase by RP-HPLC and SE-HPLC

2005 ◽  
Vol 63 (2) ◽  
pp. 111-124 ◽  
Author(s):  
Wanmeng Mu ◽  
Dongfang Zhang ◽  
Lei Xu ◽  
Zhaofeng Luo ◽  
Yuzhen Wang
Keyword(s):  
Activity Assay ◽  
Dna Photolyase ◽  
E Coli ◽  
Rp Hplc

DNA photolyase of enterococci: possible explanation for its low sunlight inactivation rate

Biologia ◽  
2009 ◽  
Vol 64 (5) ◽  
Author(s):  
Mushtaq Hussain ◽  
Syeda Qamarunnissa ◽  
Saboohi Raza ◽  
Javed Qureshi ◽  
Abdul Wajid ◽  
...  
Keyword(s):  
Binding Sites ◽  
Light Harvesting ◽  
Inactivation Rate ◽  
Dna Photolyase ◽  
Multiple Sequence ◽  
Efficient Energy Transfer ◽  
Tertiary Structures ◽  
E Coli ◽  
The Difference ◽  
Substrate Binding Sites

AbstractDNA photolyase is perhaps the most ancient and direct arsenal in curing the UV-induced dimers formed in the microbial genome. Out of two cofactors of the enzyme, catalytic and light harvesting, differences in the latter have provided basis for categorizing photolyases of prokaryotes as folate and deazaflavin types. In the present study, the homology modeling of DNA photolyase of Enterococcus faecalis was undertaken. The predicted models were structurally compared with the crystal structure coordinates of photolyases from Escherichia coli (folate type) and Anacystis nidulans (deazaflavin type). Discrepancies present in the multiple sequence alignment and tertiary structures, particularly at the light harvesting cofactor (methenyltetrahydrofolic acid, MTHF; 8-hydroxy-5-deazaflavin, 8-HDF) binding sites indicated the mechanistic nature of enterococcal photolyase. Concisely, despite the greater holistic homology with folate-type photolyase, enterococcal photolyase was characterized as deazaflavin-type. The presence of 8-HDF binding sites and groove architecture of substrate binding sites were also found supportive in this regard. The inter cofactor distance and/or orientation also implied to the efficient energy transfer in photolyase of Enterococcus in comparison with E. coli. In addition, we observed relatively high protein deformability in the enterococcal genome, which may favors the repair action of photolyase. The findings are expected to provide molecular insights into the difference in sunlight inactivation rate of two important fecal contamination indicators, namely Enterococcus and E. coli.

DNA photolyase in E. coli: effects on UV mutagenesis by plasmids expressing the phr gene

1989 ◽  
Vol 226 (4) ◽  
pp. 259-262 ◽  
Author(s):  
K. Yamamoto ◽  
R. Bockrath
Keyword(s):  
Dna Photolyase ◽  
Uv Mutagenesis ◽  
E Coli

scholarly journals Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: review and new insights from an “inverse” deuterium isotope effect

2004 ◽  
Vol 1655 ◽  
pp. 64-70 ◽  
Author(s):  
Martin Byrdin ◽  
Valérie Sartor ◽  
André P.M. Eker ◽  
Marten H. Vos ◽  
Corinne Aubert ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Isotope Effect ◽  
Deuterium Isotope Effect ◽  
Dna Photolyase ◽  
E Coli ◽  
Proton Dynamics

Preliminary Characterization of Light Harvesting in E. coli DNA Photolyase

ChemBioChem ◽  
2004 ◽  
Vol 5 (8) ◽  
pp. 1088-1094 ◽  
Author(s):  
Allison A. Henry ◽  
Ralph Jimenez ◽  
Denise Hanway ◽  
Floyd E. Romesberg
Keyword(s):  
Light Harvesting ◽  
Dna Photolyase ◽  
E Coli ◽  
Preliminary Characterization

Endotoxin Alteration of the Mucopolysaccharide Blood Vessel Coating in Rats

1974 ◽  
Vol 32 ◽  
pp. 148-149
Author(s):  
D. E. Philpott ◽  
A. Takahashi
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Salivary Gland ◽  
Carotid Artery ◽  
Basement Membrane ◽  
Coronary Vessels ◽  
Ruthenium Red ◽  
E Coli ◽  
Old Rats ◽  
The Brain

Two month, eight month and two year old rats were treated with 10 or 20 mg/kg of E. Coli endotoxin I. P. The eight month old rats proved most resistant to the endotoxin. During fixation the aorta, carotid artery, basil arartery of the brain, coronary vessels of the heart, inner surfaces of the heart chambers, heart and skeletal muscle, lung, liver, kidney, spleen, brain, retina, trachae, intestine, salivary gland, adrenal gland and gingiva were treated with ruthenium red or alcian blue to preserve the mucopolysaccharide (MPS) coating. Five, 8 and 24 hrs of endotoxin treatment produced increasingly marked capillary damage, disappearance of the MPS coating, edema, destruction of endothelial cells and damage to the basement membrane in the liver, kidney and lung.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

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