High impact information on Electrons

• The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin [1].
• Using a kinetically fast electron hole trap, N(4)-cyclopropylcytosine ((CP)C), here we show that hole migration must involve also the higher-energy pyrimidine bases [2].
• These results indicate that proton transfer from the hydroxyl group of Ser-L223 or Thr-L223 is required for fast electron and proton transfer associated with the formation of the dihydroquinone QH2 [3].
• The luminal helix l of PsaB is essential for recognition of plastocyanin or cytochrome c6 and fast electron transfer to photosystem I in Chlamydomonas reinhardtii [4].
• We have measured the first state-resolved, absolute cross sections for positron excitation of electronic states of an atom or molecule using a high resolution (Delta E approximately 25 meV FWHM) beam of positrons from a Penning-Malmberg trap [5].

Biological context of Electrons

• We propose a kinetic scheme for reductive methylation of wild-type cob(II)alamin enzyme by adenosylmethionine and flavodoxin hydroquinone in which slow conformational changes mask the relatively fast electron and methyl transfer steps [6].

Anatomical context of Electrons

• Hearts were then stained with triphenyl tetrazolium chloride (TTC) to assess the viability of the epicardium under the probe to a depth corresponding to the range of positrons [7].

Associations of Electrons with chemical compounds

• The iron-sulfur center and the flavin are about 9 A apart, which allows a fast electron transfer [8].
• NADP(H) binding is essential for fast electron transfer through the flavoprotein domain of the fusion protein P450BM3 [9].
• Tyr218 and Lys85 may have a role in the recognition/binding process for ascorbate and are indispensable for the fast electron transfer reaction [10].
• It is suggested that the detergent-induced fraction of fast electron transfer is most likely due to alteration of the environment of the quinone in the PsaA branch of cofactors and is not the result of a change in the directionality of electron transfer [11].
• The cyanide-inhibited ba3 oxidizes cyt c522 quickly (k approximately 5 x 10(6) M-1 s-1 at 25 degrees C) and selectively, with an activation energy E of 10.9 +/- 0.9 kcal mol-1, but slowly oxidizes ruthenium hexamine, a fast electron donor for the mitochondrial enzyme [12].

Gene context of Electrons

• In benzonitrile, on the other hand, the photoexcitation of the triad results in the fast electron transfer (< 1 ps) from photoexcited Zn(II)chlorin to fullerene [13].
• Diethyl pyrocarbonate modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: identification of the modification sites by mass spectrometric analysis [14].
• Fast electron transfer processes in cytochrome C and related metalloproteins [15].
• Previous studies have shown that the interaction of P450 reductase with bound NADP(H) is essential to ensure fast electron transfer through the two flavin cofactors [16].
• Cyt c2 reduces the photooxidized primary donor D+ in 0.9 +/- 0.1 micros in the co-crystals, which is the same as the fast electron transfer rate in vivo and in solution [17].

Analytical, diagnostic and therapeutic context of Electrons

• The influence of the positron distance of flight in various human tissues on the spatial resolution in positron emission tomography (PET) was assessed for positrons from carbon-11, nitrogen-13, oxygen-15, fluorine-18, gallium-68 and rubidium-82 [18].

References