An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre

Autor: Bruno Robert, Michael R. Jones, Katherine McAuley, Neil W. Isaacs, Justin P. Ridge, Paul K. Fyfe, R. van Grondelle, Richard J. Cogdell, M. E. van Brederode

Publikováno v: Biochemical Journal. 351:567-578

A series of reaction centres bearing mutations at the (Phe) M197 position were constructed in the photosynthetic bacterium Rhodobacter sphaeroides. This residue is adjacent to the pair of bacteriochlorophyll molecules (P-L and P-M) that is the primar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8c62f0fc2906e33fc5bc08caa4e03b31
https://doi.org/10.1042/bj3510567

A New Pathway for Transmembrane Electron Transfer in Photosynthetic Reaction Centers of Rhodobacter sphaeroides Not Involving the Excited Special Pair

Autor: M. R. Jones, F. van Mourik, I.H.M. van Stokkum, M. E. van Brederode, R. van Grondelle

Publikováno v: van Brederode, M E, Jones, M R, van Mourik, F, van Stokkum, I H M & van Grondelle, R 1997, ' A new pathway for transmembrane electron transfer in photosyntetic reaction centers of Rhodobacter sphaeroides not involving the excited special pair. ', Biochemistry, vol. 36, pp. 6855-6861 . https://doi.org/10.1021/bi9703756
Biochemistry, 36, 6855-6861. American Chemical Society
van Brederode, M E, Jones, M R, van Mourik, F, van Stokkum, I H M & van Grondelle, R 1997, ' A new pathway for transmembrane electron transfer in photosynthetic reaction centers of Rhodobacter sphaeroides not involving the excited special pair. ', Biochemistry, vol. 36, pp. 6855-6861 . https://doi.org/10.1021/bi9703756

It is generally accepted that electron transfer in bacterial photosynthesis is driven by the first singlet excited state of a special pair of bacteriochlorophylls (P*). We have examined the first steps of electron transfer in a mutant of the Rhodobac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::290e992fb755e40adcaf15abb4706f63
https://doi.org/10.1021/bi9703756

Protein folding thermodynamics applied to the photocycle of the photoactive yellow protein

Autor: Wouter D. Hoff, I.H.M. van Stokkum, Klaas J. Hellingwerf, M. E. van Brederode, Marie Louise Groot

Publikováno v: Biophysical Journal, 71, 365-380. Biophysical Society
van Brederode, M E, Hoff, W D, van Stokkum, I H M, Groot, M L & Hellingwerf, K J 1996, ' Protein folding thermodynamics applied to the photocycle of photoactive yellow protein. ', Biophysical Journal, vol. 71, pp. 365-380 . https://doi.org/10.1016/S0006-3495(96)79234-2

Two complementary aspects of the thermodynamics of the photoactive yellow protein (PYP), a new type of photoreceptor that has been isolated from Ectothiorhodospira halophila, have been investigated. First, the thermal denaturation of PYP at pH 3.4 ha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c842528f5623c5ee55dd2d327299273c
https://doi.org/10.1016/s0006-3495(96)79234-2

Measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila

Autor: I.H.M. van Stokkum, Wouter D. Hoff, J. C. Fitch, H.J. van Ramesdonk, Terry E. Meyer, Albert M. Brouwer, M. E. van Brederode, R. van Grondelle, Klaas J. Hellingwerf

Publikováno v: Biophysical Journal, 67, 1691-1705. Biophysical Society

The photocycle of the photoactive yellow protein (PYP) from Ectothiorhodospira halophila was examined by time-resolved difference absorption spectroscopy in the wavelength range of 300-600 nm. Both time-gated spectra and single wavelength traces were

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f75c7a221a21570e5dbdcdc30818c8e9
https://doi.org/10.1016/s0006-3495(94)80643-5

An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre

Autor: J P, Ridge, P K, Fyfe, K E, McAuley, M E, van Brederode, B, Robert, R, van Grondelle, N W, Isaacs, R J, Cogdell, M R, Jones

Publikováno v: The Biochemical journal.

A series of reaction centres bearing mutations at the (Phe) M197 position were constructed in the photosynthetic bacterium Rhodobacter sphaeroides. This residue is adjacent to the pair of bacteriochlorophyll molecules (P(L) and P(M)) that is the prim

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::769e0c955fc033376fcf7442cff97584
https://pubmed.ncbi.nlm.nih.gov/11042110