COX5B

COX5B

COX5B

Protein-coding gene in the species Homo sapiens

Cytochrome c oxidase subunit 5B, mitochondrial is an enzyme in humans that is a subunit of the cytochrome c oxidase complex, also known as Complex IV, the last enzyme in the mitochondrial electron transport chain.[2] In humans, cytochrome c oxidase subunit 5B is encoded by the COX5B gene.

Quick Facts Cytochrome c oxidase subunit Vb, Identifiers ...

Structure

The enzyme weighs 14 kDa and is composed of 129 amino acids.[3][4] The protein is a subunit of Complex IV, which consists of 13 mitochondrial- and nuclear-encoded subunits.[2] The sequence of subunit Vb is well conserved and includes three conserved cysteines that coordinate the zinc ion.[5][6] Two of these cysteines are clustered in the C-terminal section of the subunit.

Gene

Quick Facts Identifiers, Aliases ...

The COX5B gene, located on the q arm of chromosome 2 in position 11.2, is made up of 4 exons and is 2,137 base pairs in length.[2]

Function

Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane to drive ATP synthesis via protonmotive force. The mitochondrially-encoded subunits perform the electron transfer of proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex.[2]

Summary reaction:

4 Fe2+-cytochrome c + 8 H+in + O2 → 4 Fe3+-cytochrome c + 2 H2O + 4 H+out[11]

Clinical significance

COX5A and COX5B are involved in the regulation of cancer cell metabolism by Bcl-2.[12]

The Trans-activator of transcription protein (Tat) of human immunodeficiency virus (HIV) inhibits cytochrome c oxidase (COX) activity in permeabilized mitochondria isolated from both mouse and human liver, heart, and brain samples.[13]

Interactions

COX5B has been shown to interact with Androgen receptor.[14]

References

  1. [1]
    Miki K, Sogabe S, Uno A, et al. (May 1994). "Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis" (PDF). Acta Crystallogr. D. 50 (Pt 3): 271–5. Bibcode:1994AcCrD..50..271M. doi:10.1107/S0907444993013952. PMID 15299438.
  2. [2]
    "Entrez Gene: COX5B cytochrome c oxidase subunit Vb".
  3. [3]
    ]Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
  4. [4]
    "Cytochrome c oxidase subunit 5B, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 2018-07-19. Retrieved 2018-07-18.
  5. [5]
    Rizzuto R, Sandona D, Brini M, Capaldi RA, Bisson R (1991). "The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideum". Biochim. Biophys. Acta. 1129 (1): 100–104. doi:10.1016/0167-4781(91)90220-G. PMID 1661610.
  6. [6]
    Tsukihara T, Yamaguchi H, Aoyama H, Yamashita E, Tomizaki T, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S (1996). "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A". Science. 272 (5265): 1136–1144. Bibcode:1996Sci...272.1136T. doi:10.1126/science.272.5265.1136. PMID 8638158. S2CID 20860573.
  7. [7]
    GRCh38: Ensembl release 89: ENSG00000135940 – Ensembl, May 2017
  8. [8]
    GRCm38: Ensembl release 89: ENSMUSG00000061518 – Ensembl, May 2017
  9. [9]
    "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  10. [10]
    "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  11. [11]
    Pratt Donald Voet, Judith G. Voet, Charlotte W. (2013). "18". Fundamentals of biochemistry : life at the molecular level (4th ed.). Hoboken, NJ: Wiley. pp. 581–620. ISBN 978-0-470-54784-7.{{cite book}}: CS1 maint: multiple names: authors list (link)
  12. [12]
    Chen ZX, Pervaiz S (Mar 2010). "Involvement of cytochrome c oxidase subunits Va and Vb in the regulation of cancer cell metabolism by Bcl-2". Cell Death and Differentiation. 17 (3): 408–20. doi:10.1038/cdd.2009.132. PMID 19834492.
  13. [13]
    Lecoeur H, Borgne-Sanchez A, Chaloin O, El-Khoury R, Brabant M, Langonné A, Porceddu M, Brière JJ, Buron N, Rebouillat D, Péchoux C, Deniaud A, Brenner C, Briand JP, Muller S, Rustin P, Jacotot E (2012). "HIV-1 Tat protein directly induces mitochondrial membrane permeabilization and inactivates cytochrome c oxidase". Cell Death & Disease. 3 (3): e282. doi:10.1038/cddis.2012.21. PMC 3317353. PMID 22419111.
  14. [14]
    Beauchemin AM, Gottlieb B, Beitel LK, Elhaji YA, Pinsky L, Trifiro MA (2001). "Cytochrome c oxidase subunit Vb interacts with human androgen receptor: a potential mechanism for neurotoxicity in spinobulbar muscular atrophy". Brain Res. Bull. 56 (3–4): 285–97. doi:10.1016/S0361-9230(01)00583-4. PMID 11719263. S2CID 24740136.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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