The three-dimensional configuration of the ester heterocycle is basically the same as that of the carbocycle. Compound: 5,5′-Dimethyl-2,2′-bipyridine(SMILESS: CC1=CN=C(C=C1)C1=NC=C(C)C=C1,cas:1762-34-1) is researched.Recommanded Product: 5,5′-Dimethyl-2,2′-bipyridine. The article 《The laser-induced potential jump: A method for rapid electron injection into oxidoreductase enzymes》 in relation to this compound, is published in Journal of Physical Chemistry B. Let’s take a look at the latest research on this compound (cas:1762-34-1).
Oxidoreductase enzymes often perform technol. useful chem. transformations using abundant metal cofactors with high efficiency under ambient conditions. The understanding of the catalytic mechanism of these enzymes is, however, highly dependent on the availability of well-characterized and optimized time-resolved anal. techniques. We have developed an approach for rapidly injecting electrons into a catalytic system using a photoactivated nanomaterial in combination with a range of redox mediators to produce a potential jump in solution, which then initiates turnover via electron transfer (ET) to the catalyst. The ET events at the nanomaterial-mediator-catalyst interfaces are, however, highly sensitive to the exptl. conditions such as photon flux, relative concentrations of system components, and pH. Here, we present a systematic optimization of these exptl. parameters for a specific catalytic system, namely, [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1). The developed strategies can, however, be applied in the study of a wide variety of oxidoreductase enzymes. Our potential jump system consists of CdSe/CdS core-shell nanorods as a photosensitizer and a series of substituted bipyridinium salts as mediators with redox potentials in the range from -550 to -670 mV (vs. SHE). With these components, we screened the effect of pH, mediator concentration, protein concentration, photosensitizer concentration, and photon flux on steady-state photoreduction and hydrogen production as well as ET and potential jump efficiency. By manipulating these exptl. conditions, we show the potential of simple modifications to improve the tunability of the potential jump for application to study oxidoreductases.
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