CASSCF//CASPT2 pathways for a two-glycine minimal model system show that photoinduced electron-driven forward and backward proton transfer could play an important role for the stability of proteins against damage by UV radiation, when a hydrogen bond is located between the two amino acids. The overall photoinduced process involves two electron and proton transfer processes (forward and backward) and results in the reformation of the initial closed-shell electronic structure of the system
The photoactive yellow protein (PYP) acts as a light sensor to its bacterial host: it responds to li...
In PhrA, a class III CPD photolyase, two branching tryptophan charge transfer pathways have been cha...
Author Institution: 191 W. Woodruff Ave., Columbus, Ohio 43210.Photolyase is a flavoprotein which ut...
Hydrogen bonding interactions between biological chromophores and their surrounding protein and solv...
Hydrogen bonding interactions between biological chromophores and their surrounding protein and solv...
The BLUF domain (sensor of blue light using flavin adenine dinucleotide) from a bacterial photorecep...
Bacteriorhodopsin (bR) is the simplest biological system for the transduction of light energy. Light...
International audienceAmino-acid radicals play key roles in many enzymatic reactions. Catalysis ofte...
BLUF domains are flavin-binding photoreceptors that can be reversibly switched from a dark-adapted s...
We present the results of a systematic series of constrained minimum energy pathway calculations on ...
Photoinduced electron transfer in biological systems, especially in proteins, is a highly intriguing...
Photoreceptor proteins control vital cellular responses to light. The photocycle of the Slr1694 blue...
Photooxidation of proteins may result from a direct reactivity of the amino acids such as tyrosin or...
The green fluorescent protein is a key technology in bioimaging. In this critical review, we conside...
The photophysical properties of the wild type green fluorescent protein (wtGFP), the isolated GFP ch...
The photoactive yellow protein (PYP) acts as a light sensor to its bacterial host: it responds to li...
In PhrA, a class III CPD photolyase, two branching tryptophan charge transfer pathways have been cha...
Author Institution: 191 W. Woodruff Ave., Columbus, Ohio 43210.Photolyase is a flavoprotein which ut...
Hydrogen bonding interactions between biological chromophores and their surrounding protein and solv...
Hydrogen bonding interactions between biological chromophores and their surrounding protein and solv...
The BLUF domain (sensor of blue light using flavin adenine dinucleotide) from a bacterial photorecep...
Bacteriorhodopsin (bR) is the simplest biological system for the transduction of light energy. Light...
International audienceAmino-acid radicals play key roles in many enzymatic reactions. Catalysis ofte...
BLUF domains are flavin-binding photoreceptors that can be reversibly switched from a dark-adapted s...
We present the results of a systematic series of constrained minimum energy pathway calculations on ...
Photoinduced electron transfer in biological systems, especially in proteins, is a highly intriguing...
Photoreceptor proteins control vital cellular responses to light. The photocycle of the Slr1694 blue...
Photooxidation of proteins may result from a direct reactivity of the amino acids such as tyrosin or...
The green fluorescent protein is a key technology in bioimaging. In this critical review, we conside...
The photophysical properties of the wild type green fluorescent protein (wtGFP), the isolated GFP ch...
The photoactive yellow protein (PYP) acts as a light sensor to its bacterial host: it responds to li...
In PhrA, a class III CPD photolyase, two branching tryptophan charge transfer pathways have been cha...
Author Institution: 191 W. Woodruff Ave., Columbus, Ohio 43210.Photolyase is a flavoprotein which ut...