COX4I2

From Wikipedia, the free encyclopedia
Jump to: navigation, search
COX4I2
Identifiers
Aliases COX4I2, COX4, COX4-2, COX4B, COX4L2, COXIV-2, dJ857M17.2, cytochrome c oxidase subunit 4I2
External IDs MGI: 2135755 HomoloGene: 13082 GeneCards: COX4I2
RNA expression pattern
PBB GE COX4I2 gnf1h00848 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_032609

NM_053091

RefSeq (protein)

NP_115998

NP_444321.1
NP_444321

Location (UCSC) Chr 20: 31.64 – 31.65 Mb Chr 2: 152.75 – 152.77 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Cytochrome c oxidase subunit 4 isoform 2, mitochondrial is an enzyme that in humans is encoded by the COX4I2 gene.[3][4][5]

Function[edit]

Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.[5]

Interactions[edit]

COX4I2 has been shown to interact with Cytochrome c.[6][7][8][9]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Hüttemann M, Kadenbach B, Grossman LI (Apr 2001). "Mammalian subunit IV isoforms of cytochrome c oxidase". Gene. 267 (1): 111–23. doi:10.1016/S0378-1119(01)00385-7. PMID 11311561. 
  4. ^ Hüttemann M, Lee I, Liu J, Grossman LI (Nov 2007). "Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element". The FEBS Journal. 274 (21): 5737–48. doi:10.1111/j.1742-4658.2007.06093.x. PMID 17937768. 
  5. ^ a b "Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)". 
  6. ^ Michel B, Bosshard HR (Aug 1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase". The Journal of Biological Chemistry. 259 (16): 10085–91. PMID 6088481. 
  7. ^ Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS (Mar 2000). "Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples". Analytical Biochemistry. 279 (1): 55–60. doi:10.1006/abio.1999.4434. PMID 10683230. 
  8. ^ Sampson V, Alleyne T (Dec 2001). "Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover". European Journal of Biochemistry / FEBS. 268 (24): 6534–44. doi:10.1046/j.0014-2956.2001.02608.x. PMID 11737208. 
  9. ^ Lynch SR, Sherman D, Copeland RA (Jan 1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase". The Journal of Biological Chemistry. 267 (1): 298–302. PMID 1309738. 

External links[edit]

Further reading[edit]

  • Lynch SR, Sherman D, Copeland RA (Jan 1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase". The Journal of Biological Chemistry. 267 (1): 298–302. PMID 1309738. 
  • Garber EA, Margoliash E (Feb 1990). "Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition". Biochimica et Biophysica Acta. 1015 (2): 279–87. doi:10.1016/0005-2728(90)90032-Y. PMID 2153405. 
  • Bolli R, Nałecz KA, Azzi A (Jan 1985). "The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase". Biochimie. 67 (1): 119–28. doi:10.1016/S0300-9084(85)80237-6. PMID 2986725. 
  • Michel B, Bosshard HR (Aug 1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase". The Journal of Biological Chemistry. 259 (16): 10085–91. PMID 6088481. 
  • Hare JF, Ching E, Attardi G (May 1980). "Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase". Biochemistry. 19 (10): 2023–30. doi:10.1021/bi00551a003. PMID 6246917. 
  • Papadopoulou LC, Tsiftsoglou AS (Sep 1996). "Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin)". Biochemical Pharmacology. 52 (5): 713–22. doi:10.1016/0006-2952(96)00349-8. PMID 8765469. 
  • Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS (Mar 2000). "Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples". Analytical Biochemistry. 279 (1): 55–60. doi:10.1006/abio.1999.4434. PMID 10683230. 
  • Sampson V, Alleyne T (Dec 2001). "Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover". European Journal of Biochemistry / FEBS. 268 (24): 6534–44. doi:10.1046/j.0014-2956.2001.02608.x. PMID 11737208. 
  • Vizirianakis IS, Pappas IS, Tsiftsoglou AS (Mar 2002). "Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells". Biochemical Pharmacology. 63 (5): 1009–17. doi:10.1016/S0006-2952(01)00937-6. PMID 11911854. 
  • Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL (Apr 2007). "HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells". Cell. 129 (1): 111–22. doi:10.1016/j.cell.2007.01.047. PMID 17418790.