Digitonin-sensitive LHCII enlarges the antenna of Photosystem I in stroma lamellae of Arabidopsis thaliana after far-red and blue-light treatment

Autor: Rob B. M. Koehorst, Emilie Wientjes, Anniek Oosterwijk, Peter Bos, Herbert van Amerongen, Arjen N. Bader, John Philippi

Publikováno v: Biochimica et Biophysica Acta-Bioenergetics 1860 (2019) 8
Biochimica et Biophysica Acta-Bioenergetics, 1860(8), 651-658

Light drives photosynthesis. In plants it is absorbed by light-harvesting antenna complexes associated with Photosystem I (PSI) and photosystem II (PSII). As PSI and PSII work in series, it is important that the excitation pressure on the two photosy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::315785081449b38bd8e559dfc373aaa3
https://doi.org/10.1016/j.bbabio.2019.07.001

Publisher Correction: Superradiance of bacteriochlorophyll c aggregates in chlorosomes of green photosynthetic bacteria

Autor: Jakub Pšenčík, David Bína, Tomáš Malina, Rob B. M. Koehorst, Herbert van Amerongen

Publikováno v: Scientific Reports, Vol 11, Iss 1, Pp 1-1 (2021)
Scientific Reports 11 (2021) 1
Scientific Reports, 11(1)
Scientific Reports

Chlorosomes are the main light-harvesting complexes of green photosynthetic bacteria that are adapted to a phototrophic life at low-light conditions. They contain a large number of bacteriochlorophyll c, d, or e molecules organized in self-assembling

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::079a473de9c99608b38c5cfb65a7cb19
https://doaj.org/article/fc117291bd1c4d9e8e3ec3a0e8780c1b

Time-Resolved Fluorescence and Fluorescence Anisotropy of Fluorescein-Labeled Poly(N-isopropylacrylamide) Incorporated in Polymersomes

Autor: Rob B. M. Koehorst, Jung Seok Lee, Herbert van Amerongen, Jan Feijen

Publikováno v: The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical 115 (2011) 45
Journal of physical chemistry B, 115(45), 13162-13167. American Chemical Society
The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 115(45), 13162-13167

The phase behavior of fluorescein isothiocyanate (FITC) labeled poly(N-isopropylacrylamide) (PNIPAAm) incorporated in polymersomes (Ps) was studied by monitoring the fluorescence lifetime (FL) and the time-resolved fluorescence anisotropy (TRFA) as a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48b6285d37d8cc9bdee628de6712863d
https://doi.org/10.1021/jp207072q

Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin

Autor: John Lee, Rob B. M. Koehorst, Willem J. H. van Berkel, Bart van Oort, Herbert van Amerongen, Natalia P. Malikova, Elena V. Eremeeva, Svetlana V. Markova, Eugene S. Vysotski, Antonie J. W. G. Visser, Sergey P. Laptenok

Publikováno v: Biochemistry, 48, 10486-10491. American Chemical Society
van Oort, B F, Eremeeva, E V, Koehorst, R B M, Laptenok, S P, van Amerongen, H, Berkel, W J H, Malikova, N P, Markova, S V, Vysotski, E S, Visser, A J W G & Lee, J 2009, ' Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin ', Biochemistry, vol. 48, pp. 10486-10491 . https://doi.org/10.1021/bi901436m
Biochemistry, 48(44), 10486-10491
Biochemistry 48 (2009) 44

Addition of calcium ions to the Ca(2+)-regulated photoproteins, such as aequorin and obelin, produces a blue bioluminescence originating from a fluorescence transition of the protein-bound product, coelenteramide. The kinetics of several transient fl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb3ebb4b3009eadd51818807215d2505
https://hdl.handle.net/1871/18993

Site-directed fluorescence labeling of a membrane protein with BADAN: probing protein topology and local environment

Autor: Rob B. M. Koehorst, Ruud B. Spruijt, Marcus A. Hemminga

Publikováno v: Biophysical Journal, 94, 3945-3955
Biophysical Journal 94 (2008)

The work presented here describes a new and simple method based on site-directed fluorescence labeling using the BADAN label that permits the examination of protein-lipid interactions in great detail. We applied this technique to a membrane-embedded,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05a6bc99d8febf7e4cacf04677475344
https://doi.org/10.1529/biophysj.107.125807