aerobic respiration II (cytochrome c) (yeast)

Feng Y, Li W, Li J, Wang J, Ge J, Xu D, Liu Y, Wu K, Zeng Q, Wu JW, Tian C, Zhou B, Yang M. Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature. 2012 Nov 15;491(7424):478–82. doi: 10.1038/nature11541. PMID: 23086143.; Smith PM, Fox JL, Winge DR. Reprint of: Biogenesis of the cytochrome bc1 complex and role of assembly factors. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 2012 Jun;1817(6):872–82. doi: 10.1016/j.bbabio.2012.03.003.; Maréchal A, Meunier B, Lee D, Orengo C, Rich PR. Yeast cytochrome c oxidase: A model system to study mitochondrial forms of the haem–copper oxidase superfamily. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 2012 Apr;1817(4):620–8. doi: 10.1016/j.bbabio.2011.08.011.; Zara V, Conte L, Trumpower BL. Biogenesis of the yeast cytochrome bc1 complex. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2009 Jan;1793(1):89–96. doi: 10.1016/j.bbamcr.2008.04.011.; Hunte C, Solmaz S, Palsdóttir H, Wenz T. A structural perspective on mechanism and function of the cytochrome bc (1) complex. Results Probl Cell Differ. 2008;45():253–78. doi: 10.1007/400_2007_042. PMID: 18038116.; Yagi T, Seo BB, Nakamaru-Ogiso E, Marella M, Barber-Singh J, Yamashita T, Kao MC, Matsuno-Yagi A. Can a single subunit yeast NADH dehydrogenase (Ndi1) remedy diseases caused by respiratory complex I defects? Rejuvenation Res. 2006;9(2):191–7. doi: 10.1089/rej.2006.9.191. PMID: 16706641.; Barnett JA. A history of research on yeasts 6: the main respiratory pathway. Yeast. 2003 Sep;20(12):1015–44. doi: 10.1002/yea.1021. PMID: 12961751.; Påhlman I, Larsson C, Averét N, Bunoust O, Boubekeur S, Gustafsson L, Rigoulet M. Kinetic Regulation of the Mitochondrial Glycerol-3-phosphate Dehydrogenase by the External NADH Dehydrogenase in Saccharomyces cerevisiae. Journal of Biological Chemistry. 2002 Aug;277(31):27991–5. doi: 10.1074/jbc.m204079200.; Lemire BD, Oyedotun KS. The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 2002 Jan;1553(1-2):102–16. doi: 10.1016/s0005-2728(01)00229-8.; Schägger H. Respiratory chain supercomplexes. IUBMB Life. 2001 Sep;52(3-5):119–28. doi: 10.1080/15216540152845911. PMID: 11798023.; Overkamp KM, Bakker BM, Ko¨tter P, van Tuijl A, de Vries S, van Dijken JP, Pronk JT. In Vivo Analysis of the Mechanisms for Oxidation of Cytosolic NADH by Saccharomyces cerevisiae Mitochondria. J Bacteriol. 2000 May 15;182(10):2823–30. doi: 10.1128/jb.182.10.2823-2830.2000.; Luttik MAH, Overkamp KM, Kötter P, de Vries S, van Dijken JP, Pronk JT. The Saccharomyces cerevisiae NDE1 and NDE2 Genes Encode Separate Mitochondrial NADH Dehydrogenases Catalyzing the Oxidation of Cytosolic NADH. Journal of Biological Chemistry. 1998 Sep;273(38):24529–34. doi: 10.1074/jbc.273.38.24529.; Geier BM, Schägger H, Ortwein C, Link TA, Hagen WR, Brandt U, Von Jagow G. Kinetic Properties and Ligand Binding of the Eleven-subunit Cytochrome-c Oxidase from Saccharomyces cerevisiae Isolated with a Novel Large-Scale Purification Method. European Journal of Biochemistry. 1995 Jan;227(1-2):296–302. doi: 10.1111/j.1432-1033.1995.tb20388.x.; DE VRIES S, VAN WITZENBURG R, GRIVELL LA, MARRES CAM. Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. European Journal of Biochemistry. 1992 Feb;203(3):587–92. doi: 10.1111/j.1432-1033.1992.tb16587.x.; Cooper CE, Nicholls P, Freedman JA. Cytochrome c oxidase: structure, function, and membrane topology of the polypeptide subunits. Biochem. Cell Biol. 1991 Sep 01;69(9):586–607. doi: 10.1139/o91-089.; MARRES CAM, de VRIES S, GRIVELL LA. Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. European Journal of Biochemistry. 1991 Feb;195(3):857–62. doi: 10.1111/j.1432-1033.1991.tb15775.x.; Capaldi RA. Structure and assembly of cytochrome c oxidase. Archives of Biochemistry and Biophysics. 1990 Aug;280(2):252–62. doi: 10.1016/0003-9861(90)90327-u.; de VRIES S, GRIVELL LA. Purification and characterization of a rotenone-insensitive NADH: Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. European Journal of Biochemistry. 1988 Sep;176(2):377–84. doi: 10.1111/j.1432-1033.1988.tb14292.x.; Daum G, Böhni PC, Schatz G. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. Journal of Biological Chemistry. 1982 Nov;257(21):13028–33. doi: 10.1016/s0021-9258(18)33617-2.; SINGER TP, MASSEY V, KEARNEY EB. Studies on succinic dehydrogenase. V. Isolation and properties of the dehydrogenase from baker's yeast. Arch Biochem Biophys. 1957 Jul;69():405–21. doi: 10.1016/0003-9861(57)90506-4. PMID: 13445213.

Metabolites

Flavone

Formula: C15H10O2 (222.06807600000002)

CAS ID: 525-82-6

H+

Formula: H (1.0078246)

CAS ID: 12408-02-5

H2O

Formula: H2O (18.0105642)

CAS ID: 7732-18-5

Oxygen

Formula: O2 (31.98983)

CAS ID: 7782-44-7

Ubiquinone-1

Formula: C14H18O4 (250.1205028)

CAS ID: 727-81-1

QH(2)

Formula: C14H20O4 (252.136152)

CAS ID: 52590-98-4

succinate(2-)

Formula: C4H4O4 (116.01095839999999)

CAS ID: 56-14-4

butenedioate

Formula: C4H2O4 (113.99530920000001)

CAS ID: 17013-01-3

NAD(1-)

Formula: C21H26N7O14P2 (662.1012936000001)

CAS ID: 53-84-9



Enzyme

EC Number name full name note
1.3.5.1 succinate dehydrogenase succinate:quinone oxidoreductase
1.6.5.9 NADH:quinone reductase (non-electrogenic) NADH:quinone oxidoreductase
7.1.1.9 cytochrome-c oxidase ferrocytochrome-c:oxygen oxidoreductase


Proteins

Protein ID name full name
P00401 COX1 Cytochrome c oxidase subunit 1
P00410 COX2 Cytochrome c oxidase subunit 2
P00420 COX3 Cytochrome c oxidase subunit 3
P21801 SDH2 Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
P32340 NDI1 Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
P40215 NDE1 External NADH-ubiquinone oxidoreductase 1, mitochondrial
Q00711 SDH1 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
Q07500 NDE2 External NADH-ubiquinone oxidoreductase 2, mitochondrial