Impossibility of obtaining a CP-violating Euler-Heisenberg effective theory from a viable modification of QED

In this paper, we examine the CP-violating term of the Euler-Heisenberg action. We focus in the aspects related with the generation of such a term from a QED-like model in terms of the effective action approach. In particular, we show that the generation of the CP-violating term is closely related with both of vector and axial fermionic bilinears. Although, these anomalous models are not a "viable" extension of QED, we argue that the CP-violating term in the photon sector is obtained only from this class of models, and not from any fundamental field theory.Comment: 6 page

Induced CP-violation in the Euler–Heisenberg Lagrangian

Abstract In this paper, we examine the behaviour of the Euler–Heisenberg effective action in the presence of a novel axial coupling among the gauge field and the fermionic matter. This axial coupling is responsible to induce a CP-violating term in the extended form of the Euler–Heisenberg effective action, which is generated naturally through the analysis of the box diagram. However, this anomalous model is not a viable extension of QED, and we explicitly show that the induced CP-violating term in the Euler–Heisenberg effective Lagrangian is obtained only by adding an axial coupling to the ordinary QED Lagrangian. In order to perform our analysis, we use a parametrization of the vector and axial coupling constants, $$g_{v}$$ g v and $$g_{a}$$ g a , in terms of a new coupling $$\beta$$ β . Interestingly, this parametrization allows us to explore a hidden symmetry under the change of $$g_{v}\leftrightarrow g_{a}$$ g v ↔ g a in some diagrams. This symmetry is explicitly observed in the analysis of the box diagram, where we determine the $$\lambda _i$$ λ i coefficients of $${\mathcal {L}}_{\mathrm{ext.}}^\mathrm{\small EH}=\lambda _{1}{\mathcal {F}}^{2}+\lambda _{2}{\mathcal {G}}^{2}+ \lambda _{3}{\mathcal {F}}{\mathcal {G}}$$ L ext . E H = λ 1 F 2 + λ 2 G 2 + λ 3 F G , specially the coefficient $$\lambda _3$$ λ 3 related with the CP-violating term due to the axial coupling. As a phenomenological application of the results, we compute the relevant cross section for the light by light scattering through the extended Euler–Heisenberg effective action

Characterization of a Mycobacterium tuberculosis Nanocompartment and Its Potential Cargo Proteins

Mycobacterium tuberculosis has evolved various mechanisms by which the bacterium can maintain homeostasis under numerous environmental assaults generated by the host immune response. M. tuberculosis harbors enzymes involved in the oxidative stress response that aid in survival during the production of reactive oxygen species in activated macrophages. Previous studies have shown that a dye-decolorizing peroxidase (DyP) is encapsulated by a bacterial nanocompartment, encapsulin (Enc), whereby packaged DyP interacts with Enc via a unique C-terminal extension. M. tuberculosis also harbors an encapsulin homolog (CFP-29, Mt-Enc), within an operon with M. tuberculosis DyP (Mt-DyP), which contains a C-terminal extension. Together these observations suggest that Mt-DyP interacts with Mt-Enc. Furthermore, it has been suggested that DyPs may function as either a heme-dependent peroxidase or a deferrochelatase. Like Mt-DyP, M. tuberculosis iron storage ferritin protein, Mt-BfrB, and an M. tuberculosis protein involved in folate biosynthesis, 7,8-dihydroneopterin aldolase (Mt-FolB), have C-terminal tails that could also interact with Mt-Enc. For the first time, we show by co-purification and electron microscopy that mycobacteria via Mt-Enc can encapsulate Mt-DyP, Mt-BfrB, and Mt-FolB. Functional studies of free or encapsulated proteins demonstrate that they retain their enzymatic activity within the Mt-Enc nanocompartment. Mt-DyP, Mt-FolB, and Mt-BfrB all have antioxidant properties, suggesting that if these proteins are encapsulated by Mt-Enc, then this nanocage may play a role in the M. tuberculosis oxidative stress response. This report provides initial structural and biochemical clues regarding the molecular mechanisms that utilize compartmentalization by which the mycobacterial cell may aid in detoxification of the local environment to ensure long term survival