Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Mitochondrial Electron Transport Chain
Homo sapiens
Metabolic Pathway
The electron transport chain in mitochondria leads to the transport of hydrogen ions across the inner membrane of the mitochndria, and this proton gradient is eventually used in the production of ATP. Electrons travel down a chain of electron carriers in the inner mitochondrial membrane, ending with oxygen.
The outer membrane of the mitochondrion is permeable to ions and other small molecules and nothing in this pathway requires a specific transporter to enter into the intermembrane space. However, the inner membrane is only permeable to water, oxygen and carbon dioxide, and all other molecules, including protons, require transport proteins. Phosphate is able to enter the mitochondrial matrix via the glucose-6-phosphate translocase, and ADP is able to enter the matrix as ATP leaves it via the ADP/ATP translocase 1 protein.
Electrons donated by NADH can enter the electron transport chain as NADH dehydrogenase, known as complex I, facilitates their transfer to ubiquinone, also known as coenzyme Q10. As this occurs, the coenzyme Q10 becomes reduced to form ubiquinol, and protons are pumped from the intermembrane space to the matrix.
Lower energy electrons can also be donated to complex II, which includes succinate dehydrogenase and contains FAD. These electrons move from succinic acid to the FAD in the enzyme complex, and then to coenzyme Q10, which is reduced to ubiquinol. Throughout this, succinic acid from the citric acid cycle is converted to fumaric acid, which then returns to the citric acid cycle. This step, unlike the others in the electron transport chain, does not result in any protons being pumped from the matrix to the intermembrane space.
Regardless of which complex moved the electrons to coenzyme Q10, the cytochrome b-c1 complex, also known as complex III, catalyzes the movement of electrons from ubiquinol to cytochrome c, oxidizing ubiquinol to ubiquinone and reducing cytochrome c. This process also leads to the pumping of hydrogen ions into the intermembrane space.
Finally, the transfer of electrons from the reduced cytochrome c is catalyzed by cytochrome c oxidase, also known as complex IV of the electron transport chain. This reaction oxidizes cytochrome c for further electron transport, and transfers the electrons to oxygen, forming molecules of water. This reaction also allows protons to be pumped across the membrane.
The proton gradient that is built up through the electron transport chain allows protons to flow through the ATP synthase proteins in the mitochondrial inner membrane, providing the energy required to synthesize ATP from ADP.
References
Mitochondrial Electron Transport Chain References
Lehninger, A.L. Lehninger principles of biochemistry (4th ed.) (2005). New York: W.H Freeman.
Salway, J.G. Metabolism at a glance (3rd ed.) (2004). Alden, Mass.: Blackwell Pub.
Guo R, Gu J, Zong S, Wu M, Yang M: Structure and mechanism of mitochondrial electron transport chain. Biomed J. 2018 Feb;41(1):9-20. doi: 10.1016/j.bj.2017.12.001. Epub 2018 Mar 26.
Pubmed: 29673555
Abrahams JP, Leslie AG, Lutter R, Walker JE: Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature. 1994 Aug 25;370(6491):621-8. doi: 10.1038/370621a0.
Pubmed: 8065448
Acin-Perez R, Fernandez-Silva P, Peleato ML, Perez-Martos A, Enriquez JA: Respiratory active mitochondrial supercomplexes. Mol Cell. 2008 Nov 21;32(4):529-39. doi: 10.1016/j.molcel.2008.10.021.
Pubmed: 19026783
Boumans H, Grivell LA, Berden JA: The respiratory chain in yeast behaves as a single functional unit. J Biol Chem. 1998 Feb 27;273(9):4872-7. doi: 10.1074/jbc.273.9.4872.
Pubmed: 9478928
Schagger H, Cramer WA, von Jagow G: Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal Biochem. 1994 Mar;217(2):220-30. doi: 10.1006/abio.1994.1112.
Pubmed: 8203750
Schagger H, Pfeiffer K: Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 2000 Apr 17;19(8):1777-83. doi: 10.1093/emboj/19.8.1777.
Pubmed: 10775262
Lenaz G, Fato R, Di Bernardo S, Jarreta D, Costa A, Genova ML, Parenti Castelli G: Localization and mobility of coenzyme Q in lipid bilayers and membranes. Biofactors. 1999;9(2-4):87-93.
Pubmed: 10416019
Bianchi C, Fato R, Genova ML, Parenti Castelli G, Lenaz G: Structural and functional organization of Complex I in the mitochondrial respiratory chain. Biofactors. 2003;18(1-4):3-9.
Pubmed: 14695915
Calhoun MW, Thomas JW, Gennis RB: The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci. 1994 Aug;19(8):325-30. doi: 10.1016/0968-0004(94)90071-x.
Pubmed: 7940677
Highlighted elements will appear in red.
Highlight Compounds
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data
Settings