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Electron transfer by domain movement in cytochrome bc1
X-ray crystal structures of the cytochrome bc1 complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein. Expand
Structure and function of cytochrome bc complexes.
The cytochrome bc complexes represent a phylogenetically diverse group of complexes of electron-transferring membrane proteins, most familiarly represented by the mitochondrial and bacterial bc1Expand
The cytochrome bc1 complex: function in the context of structure.
  • A. Crofts
  • Chemistry, Medicine
  • Annual review of physiology
  • 12 February 2004
Recent advances in the understanding of the mechanism of the bc1 complex and their relation to physiologically important issues are reviewed in the context of the structural information available. Expand
Impact of folivory on photosynthesis is greater than the sum of its holes
An instrument for imaging chlorophyll fluorescence was developed and used to map the effects of caterpillar feeding on whole-leaf photosynthesis in wild parsnip, and the size of the indirect effects was positively correlated with defense-related synthesis of furanocoumarins, suggesting that costs of chemical defense may be one factor that accounts for the indirectly effects of herbivory on plants. Expand
Thermoluminescence as a probe of Photosystem II photochemistry. The origin of the flash-induced glow peaks
A single flash given at − 15°C to chloroplasts results in charge separation in Photosystem II to form a stable state which, upon warming, recombines giving rise to luminescence. This recombinationExpand
Pathways for proton release during ubihydroquinone oxidation by the bc(1) complex.
  • A. Crofts, S. Hong, +4 authors E. Berry
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 31 August 1999
From the structure of the stigmatellin-containing mitochondrial complex, it is suggested that hydrogen bonds to the two quinol hydroxyl groups help to stabilize the enzyme-substrate complex and aid proton release and that the carboxylate function is essential for rapid turnover. Expand
Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem II.
In dark-adapted chloroplasts, a damped binary oscillation as a function of flash number was observed in the kinetics of the decay of the fluorescence yield, and the relative redox potentials of the couples B/B- and B-/B2-, and the role of the component which titrates in at Eh greater than 350 mV are discussed. Expand
The Iron-Quinone Acceptor Complex
The flux of reducing equivalents out of Photosystem II (PS II) occurs through the two-electron gate function catalyzed by the iron-quinone complex on the acceptor side. The mechanism of theExpand