Isolated violaxanthin-chlorophyll a binding protein of Nannochloropsis oceanica was studied by optical spectroscopy, putting a specific focus on time-resolved fluorescence spectroscopy. Thereby, dynamic and kinetic information about the pigment-protein interactions with respect to non-photochemical quenching was collected utilizing pigment and intrinsic tryptophan fluorescence. Using this method, the investigation of the molecular environment of the pigment-protein complex during the process of qE was possible.
Anotace v angličtině
Isolated violaxanthin-chlorophyll a binding protein of Nannochloropsis oceanica was studied by optical spectroscopy, putting a specific focus on time-resolved fluorescence spectroscopy. Thereby, dynamic and kinetic information about the pigment-protein interactions with respect to non-photochemical quenching was collected utilizing pigment and intrinsic tryptophan fluorescence. Using this method, the investigation of the molecular environment of the pigment-protein complex during the process of qE was possible.
Isolated violaxanthin-chlorophyll a binding protein of Nannochloropsis oceanica was studied by optical spectroscopy, putting a specific focus on time-resolved fluorescence spectroscopy. Thereby, dynamic and kinetic information about the pigment-protein interactions with respect to non-photochemical quenching was collected utilizing pigment and intrinsic tryptophan fluorescence. Using this method, the investigation of the molecular environment of the pigment-protein complex during the process of qE was possible.
Anotace v angličtině
Isolated violaxanthin-chlorophyll a binding protein of Nannochloropsis oceanica was studied by optical spectroscopy, putting a specific focus on time-resolved fluorescence spectroscopy. Thereby, dynamic and kinetic information about the pigment-protein interactions with respect to non-photochemical quenching was collected utilizing pigment and intrinsic tryptophan fluorescence. Using this method, the investigation of the molecular environment of the pigment-protein complex during the process of qE was possible.