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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 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 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 C1

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

    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

    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