Publications by authors named "E Margoliash"

Hydrogen peroxide (H(2)O(2)) is the major reactive oxygen species (ROS) produced in sperm. High concentrations of H(2)O(2) in sperm induce nuclear DNA fragmentation and lipid peroxidation and result in cell death. The respiratory chain of the mitochondrion is one of the most productive ROS generating systems in sperm, and thus the destruction of ROS in mitochondria is critical for the cell.

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Article Synopsis
  • Ferrous cytochrome c does not bind ligands like cyanide and CO, leading to a study using cyclic voltammetry to determine its redox potential (-240 mV vs SHE).
  • The binding constant for cyanide to reduced cytochrome c was estimated to be 4.7 x 10(-3) L M(-1), indicating that it's significantly less favorable than in ferricytochrome c due to an enthalpic barrier.
  • The investigation revealed that the main issue with cyanide binding to ferrous cytochrome c is related to its compact structure and decreased conformational flexibility, influenced by various biophysical factors.
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We investigated the electron transfer (ET) rates between a well-defined gold electrode and cytochrome c immobilized at the carboxylic acid terminus of alkanethiol self-assembled monolayers (SAMs) by using the potential modulated electroreflectance technique. A logarithmic plot of ET rates against the chain length of the alkanethiol is linear with long chain alkanethiols. The ET rates become independent of the chain length with short alkanethiols.

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Cytochrome c released from vertebrate mitochondria engages apoptosis by triggering caspase activation. We previously reported that, whereas cytochromes c from higher eukaryotes can activate caspases in Xenopus egg and mammalian cytosols, iso-1 and iso-2 cytochromes c from the yeast Saccharomyces cerevisiae cannot. Here we examine whether the inactivity of the yeast isoforms is related to a post-translational modification of lysine 72, N-epsilon-trimethylation.

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Using the voltammetric method of square-wave voltammetry, a direct electrochemical examination was made of the wild type and Tyr67Phe mutant of both rat cytochrome c and yeast iso-1-cytochrome c. In addition to determining the equilibrium reduction potential (E0') for each cytochrome, the entropy of reaction, deltaS0'(Rxn)(deltaS0'(Rxn) = S0'(Red) - S0'(Ox)), for the reduction process was determined via the non-isothermal method. Having determined deltaS0'(Rxn) and E0', deltaH0' was calculated.

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