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The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Manganese cytochrome c. Structure and properties.

L C Dickinson, J C Chien

    The Journal of Biological Chemistry
    |September 10, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Synthesized manganese cytochromes c (Mn Cyt c) exhibit unique properties, including rapid autooxidation and specific ligand binding. These findings suggest a five-coordinate metalloporphyrin structure with manganese significantly out-of-plane.

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    Area of Science:

    • Biochemistry
    • Bioinorganic Chemistry
    • Spectroscopy

    Background:

    • Cytochromes c are crucial electron transfer proteins.
    • Manganese-substituted cytochromes offer insights into metalloprotein function.

    Purpose of the Study:

    • To synthesize and characterize oxidized and reduced manganese cytochromes c (Mn Cyt c+ and Mn Cyt c).
    • To investigate the physical, chemical, and enzymic properties of Mn Cyt c and Mn Cyt c+.

    Main Methods:

    • Synthesis of Mn Cyt c+ and Mn Cyt c.
    • Electrophoretic and ion exchange mobility studies.
    • Ligand binding assays (F-, CN-, N3-, CO, O2).
    • Electron paramagnetic resonance (EPR) spectroscopy.
    • Redox potential measurements.
    • Enzymic activity assays.

    Main Results:

    • Mn Cyt c+ and Fe Cyt c+ share identical mobilities.
    • Mn Cyt c rapidly autooxidizes in the presence of O2.
    • Manganese ion dissociates at acidic pH.
    • Both forms are high-spin complexes.
    • Mn Cyt c reacts reversibly with NO, forming Mn Cyt c (NO)+.
    • Half-reduction potential of Mn Cyt c is +60 ± 40 mV.
    • No interaction with cytochrome oxidase, NADH, NADPH, or succinate cytochrome reductase.

    Conclusions:

    • Manganese cytochromes c possess distinct properties compared to native cytochromes c.
    • The results suggest a five-coordinate metalloporphyrin prosthetic group.
    • The manganese ion is likely positioned significantly out-of-plane, near His-18.