| Plastocyanin conformation. An analysis of its near ultraviolet absorption and circular dichroic spectra Biophysical Journal, Volume 49, Issue 4, 1 April 1986, Pages 891-900 J.E. Draheim, G.P. Anderson, J.W. Duane and E.L. Gross Abstract The near-ultraviolet absorption and circular dichroic spectra of plastocyanin are dependent upon the redox state, solution pH, and ammonium sulfate concentration. This dependency was observed in plastocyanin isolated from spinach, poplar, and lettuce. Removal of the copper atom also perturbed the near-ultraviolet spectra. Upon reduction there are increases in both extinction and ellipticity at 252 nm. Further increases at 252 nm were observed upon formation of apo plastocyanin eliminating charge transfer transitions as the cause. The spectral changes in the near-ultraviolet imply a flexible tertiary conformation for plastocyanin. There are at least two charge transfer transitions at approximately 295–340 nm. One of these transitions is sensitive to low pH's and is attributed to the His 87 copper ligand. The redox state dependent changes observed in the near-ultraviolet spectra of plastocyanin are attenuated either by decreasing the pH to 5 or by increasing the ammonium sulfate concentration to 2.7 M. This attenuation cannot be easily explained by simple charge screening. Hydrophobic interactions probably play an important role in this phenomenon. The pH and redox state dependent conformational changes may play an important role in regulating electron transport. Abstract | PDF (1371 kb) |
| The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics Structure, Volume 6, Issue 3, 15 March 1998, Pages 323-335 Marcellus Ubbink, Mikael Ejdebäck, B Göran Karlsson and Derek S Bendall Summary The combined use of diamagnetic and paramagnetic chemical shift changes makes it possible to obtain detailed information about the structure of a transient complex of redox proteins. The structure suggests that the electrostatic interactions ‘guide’ the partners into a position that is optimal for electron transfer, and which may be stabilised by short-range interactions. Summary | Full Text | PDF (1053 kb) |
| Higher plants contain a modified cytochrome c6 Trends in Plant Science, Volume 7, Issue 6, 1 June 2002, Pages 244-245 Jürgen Wastl, Derek S Bendall and Christopher J Howe Full Text | PDF (36 kb) |
Copyright © 1972 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 12, Issue 7, 909-921, 1 July 1972
doi:10.1016/S0006-3495(72)86133-2
Electron Transfers and Components
David C. Fork
Fraction 2 (grana-stack) particles prepared with the French press showed absorbance changes, at room temperature and with sodium ascorbate and methyl-viologen, that were produced by the oxidation of cytochrome b-559. This oxidation was inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) and sensitized by system II of photosynthesis. The oxidation is too slow to account for the rates of the Hill reaction that have been observed with nicotinamide-adenine dinucleotide phosphate (NADP+). It appears that this cytochrome is not functioning in the main pathway of electron transport. In the presence of 2,3,5,6-tetramethyl-p-phenylene-diamine (DAD) and ascorbate, light-induced oxidation of cytochrome f took place within 3 msec (or faster) in the grana-stack particles. Treatment with the detergent Triton X-100 disrupted this rapid cytochrome f oxidation as well as the oxidation of cytochrome b-559. Subsequent plastocyanin addition did not restore the rapid oxidation of cytochrome f (nor of cytochrome b-559) but only slow changes of cytochrome f. In view of the fact that these particles contain almost no plastocyanin, it is unlikely that plastocyanin functions in electron transport between cytochrome f and P-700 in the particles derived from the grana-stack regions of the chloroplast.