AI Article Synopsis
- The Flavocytochrome P450 BM3 FMN domain is distinct in not producing a stable neutral blue FMN semiquinone radical like other flavodoxins.
- In anaerobic conditions, it generates a slow-disproportionating anionic red semiquinone, with a considerable impact of pH on the rate of this process.
- The reduction potential for the oxidized-semiquinone couple is -240mV, showing minimal pH dependence, which suggests that a slow protonation event helps stabilize the semiquinone, allowing it to serve as a low-potential electron donor.
Article Abstract
Flavocytochrome P450 BM3 FMN domain is unique among the family of flavodoxins and homologues, in not forming a stable neutral blue FMN semiquinone radical. Anaerobic, one-electron reduction of the isolated domain over the pH 7-9.5 range showed that it forms an anionic red semiquinone that disproportionates slowly (0.014s(-1) at pH 7). The rate of disproportionation decreased at higher pH, indicating that protonation of the anionic semiquinone is an important feature of the mechanism. The reduction potential for the oxidised-semiquinone couple was determined to be -240mV and was largely independent of pH. The semiquinone appears, therefore, to be kinetically trapped by a slow protonation event, enabling it to act as a low-potential electron donor to the P450 heme.
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| http://dx.doi.org/10.1016/j.bbrc.2004.10.189 | DOI Listing |
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