Nanosecond gating of superconducting nanowire single-photon detectors using cryogenic bias circuitry.

Superconducting nanowire single-photon detectors (SNSPDs) show near unity efficiency, low dark count rate, and short recovery time. Combining these characteristics with temporal control of SNSPDs broadens their applications as in active de-latching for higher dynamic range counting or temporal filtering for pump-probe spectroscopy or LiDAR. To that end, we demonstrate active gating of an SNSPD with a minimum off-to-on rise time of 2.4 ns and a total gate length of 5.0 ns. We show how the rise time depends on the inductance of the detector in combination with the control electronics. The gate window is demonstrated to be fully and freely, electrically tunable up to 500 ns at a repetition rate of 1.0 MHz, as well as ungated, free-running operation. Control electronics to generate the gating are mounted on the 2.3 K stage of a closed-cycle sorption cryostat, while the detector is operated on the cold stage at 0.8 K. We show that the efficiency and timing jitter of the detector is not altered during the on-time of the gating window. We exploit gated operation to demonstrate a method to increase in the photon counting dynamic range by a factor 11.2, as well as temporal filtering of a strong pump in an emulated pump-probe experiment.

Quantum detector tomography of a 2×2 multi-pixel array of superconducting nanowire single photon detectors.

We demonstrate quantum detector tomography of a commercial 2×2 array of superconducting nanowire single photon detectors. We show that detector-specific figures of merit including efficiency, dark-count and cross-talk probabilities can be directly extracted, without recourse to the underlying detector physics. These figures of merit are directly identified from just four elements of the reconstructed positive operator valued measure (POVM) of the device. We show that the values for efficiency and dark-count probability extracted by detector tomography show excellent agreement with independent measurements of these quantities, and we provide an intuitive operational definition for cross-talk probability. Finally, we show that parameters required for the reconstruction must be carefully chosen to avoid oversmoothing the data.

Mitochondrial OXA Translocase Plays a Major Role in Biogenesis of Inner-Membrane Proteins.

The mitochondrial inner membrane harbors three protein translocases. Presequence translocase and carrier translocase are essential for importing nuclear-encoded proteins. The oxidase assembly (OXA) translocase is required for exporting mitochondrial-encoded proteins; however, different views exist about its relevance for nuclear-encoded proteins. We report that OXA plays a dual role in the biogenesis of nuclear-encoded mitochondrial proteins. First, a systematic analysis of OXA-deficient mitochondria led to an unexpected expansion of the spectrum of OXA substrates imported via the presequence pathway. Second, biogenesis of numerous metabolite carriers depends on OXA, although they are not imported by the presequence pathway. We show that OXA is crucial for the biogenesis of the Tim18-Sdh3 module of the carrier translocase. The export translocase OXA is thus required for the import of metabolite carriers by promoting assembly of the carrier translocase. We conclude that OXA is of central importance for the biogenesis of the mitochondrial inner membrane.

The mitochondrial protein import machinery has multiple connections to the respiratory chain.

The mitochondrial inner membrane harbors the complexes of the respiratory chain and protein translocases required for the import of mitochondrial precursor proteins. These complexes are functionally interdependent, as the import of respiratory chain precursor proteins across and into the inner membrane requires the membrane potential. Vice versa the membrane potential is generated by the proton pumping complexes of the respiratory chain. Besides this basic codependency four different systems for protein import, processing and assembly show further connections to the respiratory chain. The mitochondrial intermembrane space import and assembly machinery oxidizes cysteine residues within the imported precursor proteins and is able to donate the liberated electrons to the respiratory chain. The presequence translocase of the inner membrane physically interacts with the respiratory chain. The mitochondrial processing peptidase is homologous to respiratory chain subunits and the carrier translocase of the inner membrane even shares a subunit with the respiratory chain. In this review we will summarize the import of mitochondrial precursor proteins and highlight these special links between the mitochondrial protein import machinery and the respiratory chain. This article is part of a Special Issue entitled: Respiratory complex II: Role in cellular physiology and disease.

Structural basis for the function of Tim50 in the mitochondrial presequence translocase.

Many mitochondrial proteins are synthesized as preproteins carrying amino-terminal presequences in the cytosol. The preproteins are imported by the translocase of the outer mitochondrial membrane and the presequence translocase of the inner membrane. Tim50 and Tim23 transfer preproteins through the intermembrane space to the inner membrane. We report the crystal structure of the intermembrane space domain of yeast Tim50 to 1.83 Å resolution. A protruding ß-hairpin of Tim50 is crucial for interaction with Tim23, providing a molecular basis for the cooperation of Tim50 and Tim23 in preprotein translocation to the protein-conducting channel of the mitochondrial inner membrane.