Electrochemical, photoelectrochemical, electrocatalytic and catalytic reduction of redox proteins

Redox proteins catalyse the reactions of a wide variety of otherwise intractable substrates, such as dinitrogen, alkanes, arenes, terpenes and steroids. Two major factors impede the utilization of these enzymes--the inefficient electron transfer between the enzyme and electrode, and the properties often, but not inevitably, associated with enzymes, such as instability, complexity, and expense. We have now shown that the former can be overcome and that proteins can be coupled, via electrodes, to a number of energy sources; the latter is the subject of much effort elsewhere. We demonstrated previously that certain redox proteins can be reduced very efficiently electrochemically (Fig. 1a). Light and hydrogen are the two other convenient energy sources that could be used for such reductions, and we now report the reduction of cytochrome c by these means.     

Does Q beta replicase synthesize RNA in the absence of template?

Q beta replicase, in the absence of added template, will synthesize RNA autocatalytically. A variety of small RNa species, termed '6S RNAs' are generated. As this reaction purportedly occurs in the absence of template, it has been termed 'de novo' RNA synthesis. The question of whether Q beta replicase can polymerize replicatable RNA molecules, without instruction from a template, has important evolutionary implications. The finding that Q beta replicase was able to synthesize RNA de novo was based on (1) failure to find contaminating RNA in Q beta replicase preparations; (2) differences in the sizes of products of apparently identical reactions; and (3) kinetic differences between template-instructed and de novo reactions. Here wer describe a procedure for production of Q beta replicase lacking one of its subunits, ribosomal protein S1, involving column chromatography in the presence of a low concentration of urea. We show that the resulting highly purified enzyme will not synthesize detectable RNA in the absence of added template. We show also that the ability to perform a reaction kinetically indistinguishable from the de novo synthesis reaction can be restored to the highly purified enzyme by adding a heat-stable, alkali-labile component of Q beta replicase preparations. Thus our findings suggest that, in the novo reaction, Q beta replicase is replicating previously undetected contaminating RNA molecules.     

The gene lin-3 encodes an inductive signal for vulval development in C. elegans.

The lin-3 gene is necessary for induction of the Caenorhabditis elegans vulva by the anchor cell. It encodes a molecule similar to epidermal growth factor and to transforming growth factor-alpha and acts through the epidermal growth factor receptor homologue let-23. Expression of lin-3 in the anchor cell stimulates vulval induction; lin-3 may encode the vulval inducing signal.     

Ametropic efficiency of visual pathway neurons

Zusammenfassung Bestimmung der Auswirkung von artefiziellen Refraktionsanomalien auf die Aktivität von Neuren in primären Sehzentren.

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This work was supported by U.S.P.H.S. Grant No. EY00576.     

GABA-mimetic action of etomidate

Summary A comparison of antagonism by bicuculline or strychnine of the effects of GABA or etomidate on rat isolated superior cervical ganglia, frog isolated hemisected spinal cords and rat central neurones in vivo indicates that etomidate has GABA-mimetic actions.Acknowledgments. This work was supported by the Medical Research Council and etomidate was provided by Janssen Pharmaceutica.