Explore: Cytochrome C.

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Source: The Open Library

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1Cytochromes c

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“Cytochromes c” Metadata:

  • Title: Cytochromes c
  • Author:
  • Language: English
  • Number of Pages: Median: 282
  • Publisher: Springer-Verlag
  • Publish Date:
  • Publish Location: New York - Berlin

“Cytochromes c” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1987
  • Is Full Text Available: Yes
  • Is The Book Public: No
  • Access Status: Borrowable

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2Proton nuclear magnetic resonance studies of the protein-protein redox complex of cytochrome c peroxidase and cytochrome c

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“Proton nuclear magnetic resonance studies of the protein-protein redox complex of cytochrome c peroxidase and cytochrome c” Metadata:

  • Title: ➤  Proton nuclear magnetic resonance studies of the protein-protein redox complex of cytochrome c peroxidase and cytochrome c
  • Author:
  • Language: English
  • Number of Pages: Median: 139
  • Publish Date:

“Proton nuclear magnetic resonance studies of the protein-protein redox complex of cytochrome c peroxidase and cytochrome c” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1994
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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3Cytochromes b and c

Book's cover

“Cytochromes b and c” Metadata:

  • Title: Cytochromes b and c
  • Number of Pages: Median: 268
  • Publisher: Nova Science Pub Inc
  • Publish Date:

“Cytochromes b and c” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 2014
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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The book is not public therefore the download links will not allow the download of the entire book, however, borrowing the book online is available.

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    4Non-mitochondrial cytochrome c

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    “Non-mitochondrial cytochrome c” Metadata:

    • Title: Non-mitochondrial cytochrome c
    • Authors:
    • Language: English
    • Number of Pages: Median: 85
    • Publisher: Elsevier
    • Publish Date:
    • Publish Location: Amsterdam, The Netherlands

    “Non-mitochondrial cytochrome c” Subjects and Themes:

    Edition Identifiers:

    Access and General Info:

    • First Year Published: 1991
    • Is Full Text Available: No
    • Is The Book Public: No
    • Access Status: No_ebook

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    Wiki

    Source: Wikipedia

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    Cytochrome c

    The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion, where it plays a critical

    Cytochrome c oxidase

    The enzyme cytochrome c oxidase or Complex IV (was EC 1.9.3.1, now reclassified as a translocase EC 7.1.1.9) is a large transmembrane protein complex found

    Cytochrome

    Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox

    Coenzyme Q – cytochrome c reductase

    The coenzyme Q : cytochrome c – oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the

    Cytochrome c peroxidase

    Cytochrome c peroxidase, or CCP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c

    Cytochrome c oxidase subunit III

    Cytochrome c oxidase subunit III (COX3) is an enzyme that in humans is encoded by the MT-CO3 gene. It is one of main transmembrane subunits of cytochrome

    Cytochrome c oxidase subunit 2

    Cytochrome c oxidase II is a protein in eukaryotes that is encoded by the MT-CO2 gene. Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII

    Cytochrome c oxidase subunit I

    Cytochrome c oxidase I (COX1) also known as mitochondrially encoded cytochrome c oxidase I (MT-CO1) is a protein that is encoded by the MT-CO1 gene in

    Cytochrome C1

    to cytochrome c in the mitochondrial respiratory chain. It is formed in the cytosol and targeted to the mitochondrial intermembrane space. Cytochrome c1

    Oxidative phosphorylation

    two molecules of cytochrome c, the efficiency would be halved, with only one proton transferred per cytochrome c reduced. Cytochrome c oxidase, also known