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Dodecins, a group of flavin-binding proteins with a dodecameric quaternary structure, are able to incorporate two flavins within each of their six identical binding pockets building an aromatic tetrade with two tryptophan residues. Dodecin from the archaeal Halobacterium salinarum is a riboflavin storage device. We demonstrate that unwanted side reactions induced by reactive riboflavin species and degradation of riboflavin are avoided by ultrafast depopulation of the reactive excited state of riboflavin. Intriguingly, in this process, the staggered riboflavin dimers do not interact in ground and photoexcited states. Rather, within the tetrade assembly, each riboflavin is kept under the control of the respective adjacent tryptophan, which suggests that the stacked arrangement is a matter of optimizing the flavin load. We further identify an electron transfer in combination with a proton transfer as a central element of the effective excited state depopulation mechanism. Structural and functional comparisons of the archaeal dodecin with bacterial homologs reveal diverging evolution. Bacterial dodecins bind the flavin FMN instead of riboflavin and exhibit a clearly different binding pocket design with inverse incorporations of flavin dimers. The different adoption of flavin changes photochemical properties, making bacterial dodecin a comparably less efficient quencher of flavins. This supports a functional role different for bacterial and archaeal dodecins.
The reduction potentials of 40 aromatic nitro compounds Rπ(NO2)n with Rπ = benzene, naphthalene, anthracene, fluorene and carbazole and n = 1 to 4 nitro groups are determined by cyclic voltammetry in DMF under aprotic conditions. The perturbation by the strongly electron accepting substituents can be rationalized via correlation with HMO eigenvalues. Based on reversibility criteria, the electrochemical behaviour is discussed and the compounds are classified with respect to reversible or irreversible one-electron transfer as well as up to 4 (quasi)-reversible reduction steps. The CV data measured can be used to predict redox reactions of aromatic nitro compounds in inert solvents.
The diphenyls MPh2 (M = Be, Mg, Zn, Cd, Hg) have been reacted with pyrazine (Pz) in tetrahydrofuran. Only the magnesium derivative undergoes electron transfer to yield the 1:1 radical complex [Pz(MgPh)]·. However, in the presence of sodium or potassium persistent 1:2 complexes [Pz(MPh)2]+. are formed with M = Be, Mg, Zn. Use of the higher homologues CdPh2 and HgPh2 leads to reduction to the metals. The 1:2 complexes have been characterized by ESR spectroscopy; metal coupling constants of 9Be, 25Mg and 67Zn could be determined in natural isotopic abundance.
Crystal and molecular structure analysis of the title compound 1, a most electron rich carbosilane, exhibits a shallow boat conformation for the cyclohexadiene ring which is shielded by four bulky Me3Si groups. Multiple hyperconjugative interaction occurs between the two non-conjugated olefinic π systems and the four rather long (192 pm) carbon-silicon o bonds which form an angle of about 34° with the assumed π axis. The HOMO destabilization caused by this unique structural arrangement explains the energetically facile formation and subsequent reactivity of the cation radical 1+ which was found to undergo oxidative desilylation to the aromatic 1,4-bis(trimethylsilyl) benzene precursor in the single electron transfer reaction with TCNE.
Escherichia coli nitrate reductase A (NarGHI) is a membrane-bound enzyme that couples quinol oxidation at a periplasmically oriented Q-site (Q(D)) to proton release into the periplasm during anaerobic respiration. To elucidate the molecular mechanism underlying such a coupling, endogenous menasemiquinone-8 intermediates stabilized at the Q(D) site (MSQ(D)) of NarGHI have been studied by high-resolution pulsed EPR methods in combination with (1)H2O/2H2O exchange experiments. One of the two non-exchangeable proton hyperfine couplings resolved in hyperfine sublevel correlation (HYSCORE) spectra of the radical displays characteristics typical from quinone methyl protons. However, its unusually small isotropic value reflects a singularly low spin density on the quinone carbon α carrying the methyl group, which is ascribed to a strong asymmetry of the MSQ(D) binding mode and consistent with single-sided hydrogen bonding to the quinone oxygen O1. Furthermore, a single exchangeable proton hyperfine coupling is resolved, both by comparing the HYSCORE spectra of the radical in 1H2O and 2H2O samples and by selective detection of the exchanged deuterons using Q-band 2H Mims electron nuclear double resonance (ENDOR) spectroscopy. Spectral analysis reveals its peculiar characteristics, i.e. a large anisotropic hyperfine coupling together with an almost zero isotropic contribution. It is assigned to a proton involved in a short ∼1.6 Å in-plane hydrogen bond between the quinone O1 oxygen and the Nδ of the His-66 residue, an axial ligand of the distal heme b(D). Structural and mechanistic implications of these results for the electron-coupled proton translocation mechanism at the Q(D) site are discussed, in light of the unusually high thermodynamic stability of MSQ(D).