WordNet

the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system
(biochemistry) a class of hemoprotein whose principal biological function is electron transfer (especially in cellular respiration)
any of the enzymes that catalyze biological oxidation

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carbonの化学記号
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/12/10 20:39:43」(JST)

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The enzyme cytochrome c oxidase, or Complex IV (EC 1.9.3.1), is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes.

It is the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. In the process, it binds four protons from the inner aqueous phase to make water, and in addition translocates four protons across the membrane, helping to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP.^[1]^[2]

Structure

Subunit I and II of Complex IV excluding all other subunits, PDB: 2EIK

The complex is a large integral membrane protein composed of several metal prosthetic sites and 14 ^[3] protein subunits in mammals. In mammals, eleven subunits are nuclear in origin, and three are synthesized in the mitochondria. The complex contains two hemes, a cytochrome a and cytochrome a₃, and two copper centers, the Cu_A and Cu_B centers.^[4] In fact, the cytochrome a₃ and Cu_B form a binuclear center that is the site of oxygen reduction. Cytochrome c, which is reduced by the preceding component of the respiratory chain (cytochrome bc1 complex, complex III), docks near the Cu_A binuclear center and passes an electron to it, being oxidized back to cytochrome c containing Fe³⁺. The reduced Cu_A binuclear center now passes an electron on to cytochrome a, which in turn passes an electron on to the cytochrome a₃-Cu_B binuclear center. The two metal ions in this binuclear center are 4.5 Å apart and coordinate a hydroxide ion in the fully oxidized state.

Crystallographic studies of cytochrome c oxidase show an unusual post-translational modification, linking C6 of Tyr(244) and the ε-N of His(240) (bovine enzyme numbering). It plays a vital role in enabling the cytochrome a₃- Cu_B binuclear center to accept four electrons in reducing molecular oxygen to water. The mechanism of reduction was formerly thought to involve a peroxide intermediate, which was believed to lead to superoxide production. However, the currently accepted mechanism involves a rapid four-electron reduction involving immediate oxygen-oxygen bond cleavage, avoiding any intermediate likely to form superoxide.^[5]

Assembly

The site of assembly is believed to occur near TOM/TIM, where complex intermediates are accessible to bind with subunits imported from cytosol. Hemes and cofactors are inserted into subunits I & II. Subunits I and IV initiate assembly. Other subunits may form sub-complex intermediates that later on, bind to others sub-complexes to form holo COX. In post-assembly modifications, the enzyme is dimerized, which is required for active/efficient enzyme action.^[6]^[7]

Complex subunits

Conserved subunits of the cytochrome oxidase c complex:^[8]^[9]

No.	Subunit name	Human protein	Protein description from UniProt	Pfam family with Human protein
1	Cox1	COX1_HUMAN	Cytochrome c oxidase subunit 1	Pfam PF00115
2	Cox2	COX2_HUMAN	Cytochrome c oxidase subunit 2	Pfam PF02790, Pfam PF00116
3	Cox3	COX3_HUMAN	Cytochrome c oxidase subunit 3	Pfam PF00510
4	Cox4i1	COX41_HUMAN	Cytochrome c oxidase subunit 4 isoform 1, mitochondrial	Pfam PF02936
5	Cox4a2	COX42_HUMAN	Cytochrome c oxidase subunit 4 isoform 2, mitochondrial	Pfam PF02936
6	Cox5a	COX5A_HUMAN	Cytochrome c oxidase subunit 5A, mitochondrial	Pfam PF02284
7	Cox5b	COX5B_HUMAN	Cytochrome c oxidase subunit 5B, mitochondrial	Pfam PF01215
8	Cox6a1	CX6A1_HUMAN	Cytochrome c oxidase subunit 6A1, mitochondrial	Pfam PF02046
9	Cox6a2	CX6A2_HUMAN	Cytochrome c oxidase subunit 6A2, mitochondrial	Pfam PF02046
10	Cox6b1	CX6B1_HUMAN	Cytochrome c oxidase subunit 6B1	Pfam PF02297
11	Cox6b2	CX6B2_HUMAN	Cytochrome c oxidase subunit 6B2	Pfam PF02297
12	Cox6c	COX6C_HUMAN	Cytochrome c oxidase subunit 6C	Pfam PF02937
13	Cox7a1	CX7A1_HUMAN	Cytochrome c oxidase subunit 7A1, mitochondrial	Pfam PF02238
14	Cox7a2	CX7A2_HUMAN	Cytochrome c oxidase subunit 7A2, mitochondrial	Pfam PF02238
15	Cox7a3	COX7S_HUMAN	Putative cytochrome c oxidase subunit 7A3, mitochondrial	Pfam PF02238
16	Cox7b	COX7B_HUMAN	Cytochrome c oxidase subunit 7B, mitochondrial	Pfam PF05392
17	Cox7c	COX7C_HUMAN	Cytochrome c oxidase subunit 7C, mitochondrial	Pfam PF02935
18	Cox7r	COX7R_HUMAN	Cytochrome c oxidase subunit 7A-related protein, mitochondrial	Pfam PF02238
19	Cox8a	COX8A_HUMAN	Cytochrome c oxidase subunit 8A, mitochondrial P	Pfam PF02285
20	Cox8c	COX8C_HUMAN	Cytochrome c oxidase subunit 8C, mitochondrial	Pfam PF02285
Assembly subunits^[10]^[11]^[12]
1	Coa1	COA1_HUMAN	Cytochrome c oxidase assembly factor 1 homolog	Pfam PF08695
2	Coa3	COA3_HUMAN	Cytochrome c oxidase assembly factor 3 homolog, mitochondrial	Pfam PF09813
3	Coa4	COA4_HUMAN	Cytochrome c oxidase assembly factor 4 homolog, mitochondrial	Pfam PF06747
4	Coa5	COA5_HUMAN	Cytochrome c oxidase assembly factor 5	Pfam PF10203
5	Coa6	COA6_HUMAN	Cytochrome c oxidase assembly factor 6 homolog	Pfam PF02297
6	Coa7	COA7_HUMAN	Cytochrome c oxidase assembly factor 7,	Pfam PF08238
7	Cox11	COX11_HUMAN	Cytochrome c oxidase assembly protein COX11 mitochondrial	Pfam PF04442
8	Cox14	COX14_HUMAN	Cytochrome c oxidase assembly protein	Pfam PF14880
9	Cox15	COX15_HUMAN	Cytochrome c oxidase assembly protein COX15 homolog	Pfam PF02628
10	Cox16	COX16_HUMAN	Cytochrome c oxidase assembly protein COX16 homolog mitochondrial	Pfam PF14138
11	Cox17	COX17_HUMAN	Cytochrome c oxidase copper chaperone	Pfam PF05051
12	Cox18^[13]	COX18_HUMAN	Mitochondrial inner membrane protein (Cytochrome c oxidase assembly protein 18)	Pfam PF02096
13	Cox19	COX19_HUMAN	Cytochrome c oxidase assembly protein	Pfam PF06747
14	Cox20	COX20_HUMAN	Cytochrome c oxidase protein 20 homolog	Pfam PF12597

Biochemistry

Summary reaction:

4 Fe²⁺-cytochrome c + 8 H⁺_in + O₂ → 4 Fe³⁺-cytochrome c + 2 H₂O + 4 H⁺_out

Two electrons are passed from two cytochrome c's, through the Cu_A and cytochrome a sites to the cytochrome a₃- Cu_B binuclear center, reducing the metals to the Fe²⁺ form and Cu⁺. The hydroxide ligand is protonated and lost as water, creating a void between the metals that is filled by O₂. The oxygen is rapidly reduced, with two electrons coming from the Fe²⁺cytochrome a₃, which is converted to the ferryl oxo form (Fe⁴⁺=O). The oxygen atom close to Cu_B picks up one electron from Cu⁺, and a second electron and a proton from the hydroxyl of Tyr(244), which becomes a tyrosyl radical: The second oxygen is converted to a hydroxide ion by picking up two electrons and a proton. A third electron arising from another cytochrome c is passed through the first two electron carriers to the cytochrome a₃- Cu_B binuclear center, and this electron and two protons convert the tyrosyl radical back to Tyr, and the hydroxide bound to Cu_B²⁺ to a water molecule. The fourth electron from another cytochrome c flows through Cu_A and cytochrome a to the cytochrome a₃- Cu_B binuclear center, reducing the Fe⁴⁺=O to Fe³⁺, with the oxygen atom picking up a proton simultaneously, regenerating this oxygen as a hydroxide ion coordinated in the middle of the cytochrome a₃- Cu_B center as it was at the start of this cycle. The net process is that four reduced cytochrome c's are used, along with 4 protons, to reduce O₂ to two water molecules.

Inhibition

Cyanide, sulfide, azide, and carbon monoxide^[14] all bind to cytochrome c oxidase, thus competitively inhibiting the protein from functioning, which results in chemical asphyxiation of cells. Methanol in methylated spirits is converted into formic acid, which also inhibits the same oxidase system. High levels of ATP can allosterically inhibit cytochrome c oxidase, binding from within the mitochondrial matrix.^[15]

Subcellular distribution

Cytochrome c oxidase has 3 subunits which are encoded by mitochondrial DNA. Of these 3 subunits encoded by mitochondrial DNA, two have been identified in extramitochondrial locations. In pancreatic acinar tissue, these subunits were found in zymogen granules. Additionally, in the anterior pituitary, relatively high amounts of these subunits were found in growth hormone secretory granules.^[16] The extramitochondrial function of these cytochrome c oxidase subunits has not yet been characterized. Besides cytochrome c oxidase subunits, extramitochondrial localization has also been observed for large numbers of other mitochondrial proteins.^[17]^[18] This raises the possibility about existence of yet unidentified specific mechanisms for protein translocation from mitochondria to other cellular destinations.^[16]^[18]^[19]

Clinical significance

Defects involving genetic mutations altering cytochrome c oxidase (COX) functionality or structure can result in severe, often fatal metabolic disorders. Such disorders usually manifest in early childhood and affect predominantly tissues with high energy demands (brain, heart, muscle). Among the many classified mitochondrial diseases, those involving dysfunctional COX assembly are thought to be the most severe.^[20]

The vast majority of COX disorders are linked to mutations in nuclear-encoded proteins referred to as assembly factors, or assembly proteins. These assembly factors contribute to COX structure and functionality, and are involved in several essential processes, including transcription and translation of mitochondrion-encoded subunits, processing of preproteins and membrane insertion, and cofactor biosynthesis and incorporation.^[21]

Currently, mutations have been identified in seven COX assembly factors: SURF1, SCO1, SCO2, COX10, COX15, COX20, COA5 and LRPPRC. Mutations in these proteins can result in altered functionality of sub-complex assembly, copper transport, or translational regulation. Each gene mutation is associated with the etiology of a specific disease, with some having implications in multiple disorders. Disorders involving dysfunctional COX assembly via gene mutations include Leigh syndrome, cardiomyopathy, leukodystrophy, anemia, and sensorineural deafness.

Histochemistry

COX histochemistry is used for mapping regional brain metabolism in animals, since there is a direct relation between enzyme activity and neuronal activity.^[22] Such brain mapping has been accomplished in spontaneous mutant mice with cerebellar disease such as reeler^[23] and a transgenic model of Alzheimer's disease.^[24] This technique has also been used to map learning activity in animal brain.^[25]

Additional images

ETC
Complex IV

References

^ Yoshikawa, Shinya; Shimada, Atsuhiro; Shinzawa-Itoh, Kyoko (2015). "Chapter 4 Respiratory Conservation of Energy with Dioxygen: Cytochrome c Oxidase". In Peter M.H. Kroneck and Martha E. Sosa Torres. Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases. Metal Ions in Life Sciences 15. Springer. pp. 89–130. doi:10.1007/978-3-319-12415-5_4.
^ Yee, Gereon M.; Tolman, William B. (2015). "Chapter 5, Section 2.3 Iron-Porphyrin/Copper Complexes as Cytochrome c Oxidase Models". In Peter M.H. Kroneck and Martha E. Sosa Torres. Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases. Metal Ions in Life Sciences 15. Springer. pp. 153–157. doi:10.1007/978-3-319-12415-5_5.
^ Balsa E, Marco R, Perales-Clemente E, Szklarczyk R, Calvo E, Landázuri MO, Enríquez JA (September 2012). "NDUFA4 is a subunit of complex IV of the mammalian electron transport chain". Cell Metab. 16 (3): 378–86. doi:10.1016/j.cmet.2012.07.015. PMID 22902835.
^ Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S (August 1995). "Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A". Science 269 (5227): 1069–74. doi:10.1126/science.7652554. PMID 7652554.
^ Voet, Donald (2010). Biochemistry. New York: J. Wiley & Sons. pp. 865–866. ISBN 0-470-57095-4.
^ Khalimonchuk O, Rödel G (December 2005). "Biogenesis of cytochrome c oxidase". Mitochondrion 5 (6): 363–88. doi:10.1016/j.mito.2005.08.002. PMID 16199211.
^ Fontanesi F, Soto IC, Horn D, Barrientos A (December 2006). "Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process". Am. J. Physiol., Cell Physiol. 291 (6): C1129–47. doi:10.1152/ajpcell.00233.2006. PMID 16760263.
^ Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH (1998). "Electron transfer by domain movement in cytochrome bc1.". Nature 392 (6677): 677–84. doi:10.1038/33612. PMID 9565029.
^ Kaila VR, Oksanen E, Goldman A, Bloch DA, Verkhovsky MI, Sundholm D, Wikström M (2011). "A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase.". Biochim Biophys Acta 1807 (7): 769–78. doi:10.1016/j.bbabio.2010.12.016. PMID 21211513.
^ Szklarczyk R, Wanschers BF, Cuypers TD, Esseling JJ, Riemersma M, van den Brand MA, Gloerich J, Lasonder E, van den Heuvel LP, Nijtmans LG, Huynen MA (2012). "Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase.". Genome Biol 13 (2): R12. doi:10.1186/gb-2012-13-2-r12. PMC 3334569. PMID 22356826.
^ Mick DU, Dennerlein S, Wiese H, Reinhold R, Pacheu-Grau D, Lorenzi I, Sasarman F, Weraarpachai W, Shoubridge EA, Warscheid B, Rehling P (2012). "MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation.". Cell 151 (7): 1528–41. doi:10.1016/j.cell.2012.11.053. PMID 23260140.
^ Kozjak-Pavlovic V, Prell F, Thiede B, Götz M, Wosiek D, Ott C, Rudel T (2014). "C1orf163/RESA1 is a novel mitochondrial intermembrane space protein connected to respiratory chain assembly.". J Mol Biol 426 (4): 908–20. doi:10.1016/j.jmb.2013.12.001. PMID 24333015.
^ Gaisne M, Bonnefoy N (2006). "The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast.". FEMS Yeast Res 6 (6): 869–82. doi:10.1111/j.1567-1364.2006.00083.x. PMID 16911509.
^ Alonso JR, Cardellach F, López S, Casademont J, Miró O (September 2003). "Carbon monoxide specifically inhibits cytochrome c oxidase of human mitochondrial respiratory chain". Pharmacol. Toxicol. 93 (3): 142–6. doi:10.1034/j.1600-0773.2003.930306.x. PMID 12969439.
^ Arnold S, Kadenbach B (October 1997). "Cell respiration s controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase.". Eur J Biochem 249: 350–254. doi:10.1111/j.1432-1033.1997.t01-1-00350.x. PMID 9363790.
^ ^a ^b Sadacharan SK, Singh B, Bowes T, Gupta RS (2005). "Localization of mitochondrial DNA encoded cytochrome c oxidase subunits I and II in rat pancreatic zymogen granules and pituitary growth hormone granules". Histochem. Cell Biol. 124 (5): 409–21. doi:10.1007/s00418-005-0056-2. PMID 16133117.
^ Gupta RS, Ramachandra NB, Bowes T, Singh B (2008). "Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10". Novartis Found. Symp. 291: 59–68; discussion 69–73, 137–40. doi:10.1002/9780470754030.ch5. PMID 18575266.
^ ^a ^b Soltys BJ, Gupta RS (2000). "Mitochondrial proteins at unexpected cellular locations: export of proteins from mitochondria from an evolutionary perspective". Int. Rev. Cytol. 194: 133–96. doi:10.1016/s0074-7696(08)62396-7. PMID 10494626.
^ Soltys BJ, Gupta RS (1999). "Mitochondrial-matrix proteins at unexpected locations: are they exported?". Trends Biochem. Sci. 24 (5): 174–7. doi:10.1016/s0968-0004(99)01390-0. PMID 10322429.
^ Pecina P, Houstková H, Hansíková H, Zeman J, Houstek J (2004). "Genetic defects of cytochrome c oxidase assembly" (PDF). Physiol Res. 53 Suppl 1: S213–23. PMID 15119951.
^ Zee JM, Glerum DM (December 2006). "Defects in cytochrome oxidase assembly in humans: lessons from yeast". Biochem. Cell Biol. 84 (6): 859–69. doi:10.1139/o06-201. PMID 17215873.
^ Wong-Riley MT (1989). "Cytochrome oxidase: an endogenous metabolic marker for neuronal activity.". Trends Neurosci. 12 (3): 94–111. doi:10.1016/0166-2236(89)90165-3. PMID 2469224.
^ Strazielle C, Hayzoun K, Derer M, Mariani J, Lalonde R (April 2006). "Regional brain variations of cytochrome oxidase activity in Relnrl-orl mutant mice.". J. Neurosci. Res. 83 (5): 821–31. doi:10.1002/jnr.20772. PMID 16511878.
^ Strazielle C, Sturchler-Pierrat C, Staufenbiel M, Lalonde R (2003). "Regional brain cytochrome oxidase activity in beta-amyloid precursor protein transgenic mice with the Swedish mutation.". Neuroscience 118 (4): 1151–63. doi:10.1016/S0306-4522(03)00037-X. PMID 12732258.
^ Conejo NM, González-Pardo H, Gonzalez-Lima F, Arias JL (2010). "Spatial learning of the water maze: progression of brain circuits mapped with cytochrome oxidase histochemistry.". Neurobiol. Learn. Mem. 93 (3): 362–71. doi:10.1016/j.nlm.2009.12.002. PMID 19969098.

External links

The Cytochrome Oxidase home page at Rice University
Interactive Molecular model of cytochrome c oxidase (Requires MDL Chime)
UMich Orientation of Proteins in Membranes families/superfamily-4
Cytochrome-c Oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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5. 先天性代謝異常：分類 inborn errors of metabolism classification

English Journal

Accurately mapping the location of the binding site for the interaction between hepatitis B virus X protein and cytochrome c oxidase III.

Li D1, Ding J2, Chen Z1, Chen Y1, Lin N1, Chen F1, Wang X1.
International journal of molecular medicine.Int J Mol Med.2015 Feb;35(2):319-24. doi: 10.3892/ijmm.2014.2018. Epub 2014 Dec 2.
The hepatitis B virus (HBV) X protein (HBx) plays an important pathogenetic role in hepatocarcinoma tumorigenesis. As HBx does not have the ability to bind to double-stranded DNA (dsDNA), protein-protein interaction is crucial for HBx functions. In a previous study, we screened a novel HBx-interac
PMID 25483779

The life cycle and molecular phylogeny of a gorgoderid trematode recorded from the mussel Nodularia douglasiae in the Yodo River, Japan.

Urabe M1, Ishibashi R2, Uehara K2.
Parasitology international.Parasitol Int.2015 Feb;64(1):26-32. doi: 10.1016/j.parint.2014.09.003. Epub 2014 Sep 9.
In 2009, a novel larval trematode of the family Gorgoderidae was found in the gonads of Nodularia douglasiae (Unionidae) from the lower reaches of the Yodo River, Osaka Prefecture, Japan. This is the first collection of trematodes in a unionid mussel in Japan. We investigated the morphology and life
PMID 25220581

Japanese Journal

Sequence and structure analysis of a mirror tRNA located upstream of the cytochrome oxidase Ⅰ mRNA in mouse mitochondria

The journal of biochemistry 159(3), 341-350, 2016-03
NAID 40020763434

Group II Intron-Mediated Trans-Splicing in the Gene-Rich Mitochondrial Genome of an Enigmatic Eukaryote, Diphylleia rotans

Genome biology and evolution 8(2), 458-466, 2016-02
NAID 120005743764

Rapid Identification of Echinococcus granulosus and E. canadensis Using High-Resolution Melting (HRM) Analysis by Focusing on a Single Nucleotide Polymorphism

Japanese Journal of Infectious Diseases 69(4), 300-305, 2016
NAID 130005165479

「シトクロムc酸化酵素」

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Cytochrome c oxidase
	The crystal structure of bovine cytochrome c oxidase in a phospholipid bilayer. The intermembrane space lies to top of the image. Adapted from PDB: 1OCC (It is a homo dimer in this structure)
Identifiers
EC number	1.9.3.1
CAS number	9001-16-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
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PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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　　[★]

英: cytochrome c oxidase, electron transport complex IV
同: シトクロムcオキシダーゼ、シトクロム酸化酵素 cytochrome oxidase、シトクロムオキシダーゼ、チトクロムc酸化酵素、電子伝達複合体IV、複合体IV complex IV、シトクロムaa3 cytochrome aa3、インドフェノラーゼ indophenolase、インドフェノール酸化酵素 indophenol oxidase

臨床関連

Leigh's disease

intelectual deterioration, weakness, ataxia, seizures, and death at a young age

「cytochrome oxidase」

　　[★]

チトクロム酸化酵素、チトクロムオキシダーゼ、シトクロム酸化酵素、シトクロムオキシダーゼ

関: cytochrome c oxidase、electron transport complex IV

「electron transport complex IV」

　　[★]

電子伝達複合体IV、複合体IV

関: cytochrome c oxidase、cytochrome oxidase

「cytochrome c oxidase deficiency」

　　[★]

チトクロムc酸化酵素欠損症、シトクロムc酸化酵素欠損症

関: cytochrome oxidase deficiency

「C」

　　[★]

炭素 carbon
シトシン cytosine
システイン cysteine
シチジン
セルシウス度摂氏 degrees Celsius degree C
産婦人科領域で「子宮外頚子宮外頚部 exocervix」を表現するための略語

「c」

　　[★]

光速, speed of light

[1] Yoshikawa, Shinya; Shimada, Atsuhiro; Shinzawa-Itoh, Kyoko (2015). "Chapter 4 Respiratory Conservation of Energy with Dioxygen: Cytochrome c Oxidase". In Peter M.H. Kroneck and Martha E. Sosa Torres. Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases. Metal Ions in Life Sciences 15. Springer. pp. 89–130. doi:10.1007/978-3-319-12415-5_4.

[2] Yee, Gereon M.; Tolman, William B. (2015). "Chapter 5, Section 2.3 Iron-Porphyrin/Copper Complexes as Cytochrome c Oxidase Models". In Peter M.H. Kroneck and Martha E. Sosa Torres. Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases. Metal Ions in Life Sciences 15. Springer. pp. 153–157. doi:10.1007/978-3-319-12415-5_5.

[pmid22902835-3] Balsa E, Marco R, Perales-Clemente E, Szklarczyk R, Calvo E, Landázuri MO, Enríquez JA (September 2012). "NDUFA4 is a subunit of complex IV of the mammalian electron transport chain". Cell Metab. 16 (3): 378–86. doi:10.1016/j.cmet.2012.07.015. PMID 22902835.

[pmid7652554-4] Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S (August 1995). "Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A". Science 269 (5227): 1069–74. doi:10.1126/science.7652554. PMID 7652554.

[isbn0-470-57095-4-5] Voet, Donald (2010). Biochemistry. New York: J. Wiley & Sons. pp. 865–866. ISBN 0-470-57095-4.

[pmid16199211-6] Khalimonchuk O, Rödel G (December 2005). "Biogenesis of cytochrome c oxidase". Mitochondrion 5 (6): 363–88. doi:10.1016/j.mito.2005.08.002. PMID 16199211.

[pmid16760263-7] Fontanesi F, Soto IC, Horn D, Barrientos A (December 2006). "Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process". Am. J. Physiol., Cell Physiol. 291 (6): C1129–47. doi:10.1152/ajpcell.00233.2006. PMID 16760263.

[pmid9565029-8] Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH (1998). "Electron transfer by domain movement in cytochrome bc1.". Nature 392 (6677): 677–84. doi:10.1038/33612. PMID 9565029.

[pmid21211513-9] Kaila VR, Oksanen E, Goldman A, Bloch DA, Verkhovsky MI, Sundholm D, Wikström M (2011). "A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase.". Biochim Biophys Acta 1807 (7): 769–78. doi:10.1016/j.bbabio.2010.12.016. PMID 21211513.

[pmid22356826-10] Szklarczyk R, Wanschers BF, Cuypers TD, Esseling JJ, Riemersma M, van den Brand MA, Gloerich J, Lasonder E, van den Heuvel LP, Nijtmans LG, Huynen MA (2012). "Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase.". Genome Biol 13 (2): R12. doi:10.1186/gb-2012-13-2-r12. PMC 3334569. PMID 22356826.

[pmid23260140-11] Mick DU, Dennerlein S, Wiese H, Reinhold R, Pacheu-Grau D, Lorenzi I, Sasarman F, Weraarpachai W, Shoubridge EA, Warscheid B, Rehling P (2012). "MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation.". Cell 151 (7): 1528–41. doi:10.1016/j.cell.2012.11.053. PMID 23260140.

[pmid24333015-12] Kozjak-Pavlovic V, Prell F, Thiede B, Götz M, Wosiek D, Ott C, Rudel T (2014). "C1orf163/RESA1 is a novel mitochondrial intermembrane space protein connected to respiratory chain assembly.". J Mol Biol 426 (4): 908–20. doi:10.1016/j.jmb.2013.12.001. PMID 24333015.

[pmid16911509-13] Gaisne M, Bonnefoy N (2006). "The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast.". FEMS Yeast Res 6 (6): 869–82. doi:10.1111/j.1567-1364.2006.00083.x. PMID 16911509.

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リンク元	「シトクロムc酸化酵素」「cytochrome oxidase」「electron transport complex IV」
拡張検索	「cytochrome c oxidase deficiency」
関連記事	「C」「c」

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案内

案内

cytochrome c oxidase