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Showing 1 to 5 of 5 for “"rubredoxin"”.

  1. Biosynthesis of Iron-Sulfur Clusters

    … of NifU and provides a second iron-binding site (rubredoxin-like Fe(III)-binding site). Cysteine residues Cys<sup>35</sup>, Cys⁶², Cys¹⁰⁶>, and a putative non-cysteine ligand of unknown origin provide coordination to the iron at this site. The significance of these iron-binding sites was also …

    vt Repository record for Biosynthesis of Iron-Sulfur Clusters (opens in a new tab)

  2. Characterization of the thioredoxin system in Methanosarcina mazei

    … of action for one of the FTRs. FTR2 harbors a rubredoxin domain, and this unit is the only rubredoxin in this organism. Superoxide reductase, an enzyme that reduces superoxide radical to hydrogen peroxide without forming oxygen, utilizes rubredoxin as the direct electron source and this enzyme …

    vt Repository record for Characterization of the thioredoxin system in Methanosarcina mazei (opens in a new tab)

  3. Predicting Kinetics of Spin-Dependent Reactions in an External Magnetic Field with Nonadiabatic Statistical Theory

    … in the active site model of the protein rubredoxin. The magnetic field effects and new approaches for calculating SOC have been implemented in the NAST software package, which uses results of electronic structure calculations to predict the transition probabilities and rate constants of …

    unr Repository record for Predicting Kinetics of Spin-Dependent Reactions in an External Magnetic Field with Nonadiabatic Statistical Theory (opens in a new tab)

  4. Mössbauer and EPR studies of iron-containing proteins

    "We have studied the iron-sulfur protein rubredoxin (Rd) and the heme protein horseradish peroxidase (HRP) using Mossbauer spectroscopy (MS) and electron paramagnetic resonance (EPR). Both methods are sensitive probes of the electronic structure of the iron at the active site of the protein. In all …

    uiuc Repository record for Mössbauer and EPR studies of iron-containing proteins (opens in a new tab)

  5. Funktionelle Charakterisierung potentieller Pathogenitätsfaktoren aus Pseudomonas aeruginosa mittels biochemischer und evolutiver Methoden

    … in dem Gen Pa5349, welches für eine Rubredoxin Reduktase kodiert. Diese Mutante zeigt eine erhöhte Sensitivität gegenüber reaktiven Sauerstoffspezies. Pa5349 konnte eine Funktion in einer Elektronentransportkette zugewiesen werden, welche eine zentrale Rolle in der Reduktion von …

    goettingen Repository record for Funktionelle Charakterisierung potentieller Pathogenitätsfaktoren aus Pseudomonas aeruginosa mittels biochemischer und evolutiver Methoden (opens in a new tab)