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    Cyto C

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    Mohib
    Cytochrome c is a small heme protein found in the inner mitochondrial membrane that plays a key role in electron transport as it carries electrons from Complex III to Complex IV. It has a highly conserved amino acid sequence among mammals and consists of around 100 amino acids. Cytochrome c accepts electrons from Coenzyme Q-cytochrome c reductase and donates them to cytochrome oxidase as part of oxidative phosphorylation. It is also involved in apoptosis when released from the mitochondria.

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    Cyto C

    Uploaded by

    Mohib
    21 views10 pages
    Cytochrome c is a small heme protein found in the inner mitochondrial membrane that plays a key role in electron transport as it carries electrons from Complex III to Complex IV. It has a highly conserved amino acid sequence among mammals and consists of around 100 amino acids. Cytochrome c accepts electrons from Coenzyme Q-cytochrome c reductase and donates them to cytochrome oxidase as part of oxidative phosphorylation. It is also involved in apoptosis when released from the mitochondria.

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    Cytochrome c is a small heme protein found in the inner mitochondrial membrane that plays a key role in electron transport as it carries electrons from Complex III to Complex IV. It has a highly conserved amino acid sequence among mammals and consists of around 100 amino acids. Cytochrome c accepts electrons from Coenzyme Q-cytochrome c reductase and donates them to cytochrome oxidase as part of oxidative phosphorylation. It is also involved in apoptosis when released from the mitochondria.

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    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    21 views10 pages

    Cyto C

    Uploaded by

    Mohib
    Cytochrome c is a small heme protein found in the inner mitochondrial membrane that plays a key role in electron transport as it carries electrons from Complex III to Complex IV. It has a highly conserved amino acid sequence among mammals and consists of around 100 amino acids. Cytochrome c accepts electrons from Coenzyme Q-cytochrome c reductase and donates them to cytochrome oxidase as part of oxidative phosphorylation. It is also involved in apoptosis when released from the mitochondria.

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    The Cytochrome complex, or cyt c is a small

    heme protein found loosely associated with the


    inner membrane of the mitochondrion.
    It belongs to the cytochrome c family of
    proteins.
    highly soluble protein, with a solubility of
    about 100 g/L and is an essential component of
    the electron transport chain.

    it carries one electron, capable of undergoing


    oxidation and reduction, but does not bind
    oxygen.
    found in plants, animals, and many unicellular
    organisms.
    small size (mol.wt.about 12,000 daltons).
    Its primary structure consists of a chain of
    about 100 amino acids. Many higher order
    organisms possess a chain of 104 amino acids.
    Its amino acid sequence is highly conserved in
    mammals differing by only a few residues. For
    example, the sequences of cytochrome c in
    humans is identical to that of a chimpanzees but
    differs more from that of a horses, and even
    more from the sequence of a shark.
    Cytochrome c accepts electrons from Complex
    III and diffuses to Complex IV (cytochrome
    oxidase), where it donates the electrons to O2,
    converting O2 to H2O.
    In humans, cytochrome c is encoded by the
    CYCS gene.
    FUNCTIONS:
    Cytochrome c is a component of the
    electron transport chain in mitochondria.
    The heme group of cytochrome c accepts
    electrons from the b-c1 complex (Coenzyme Q -
    Cyt C reductase) to the cytochrome oxidase
    complex.
    Upon release of cytochrome c to the
    cytoplasm, the protein binds apoptotic protease
    activating factor-1 (Apaf-1).
    Cytochrome c can catalyze several reactions
    such as hydroxylation and aromatic oxidation.

    In the process of oxidative phosphorylation,


    Cyt c play important role.
    Classes:
    In 1991 R. P. Ambler recognized four classes of
    cyt c:
    Class I includes the low spin soluble
    cytochrome c of mitochondria and bacteria. It
    has the heme-attachment site towards the N
    terminus of histidine and the sixth ligand
    provided by a methionine residue towards the C
    terminus.
    Class II includes the high spin cytochrome c'.
    It has the heme-attachment site closed to the N
    terminus of histidine.
    Class III comprises the low redox potential
    multiple heme cytochromes. The heme c groups
    are structurally and functionally nonequivalent
    and present different redox potentials in the
    range 0 to -400 mV.

     Class IV was originally created to hold the


    complex proteins that have other prosthetic
    groups as well as heme c.
    Applications
    Cytochrome c is suspected to be the functional
    complex in so called LLLT:
    Low-level laser therapy.
    In LLLT, red light and some near infra-red
    wavelengths penetrate tissue in order to increase
    cellular regeneration.
    Light of this wavelength appears capable of
    increasing activity of cytochrome c, thus
    increasing metabolic activity and freeing up
    more energy for the cells to repair the tissue.

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