The anaerobic enzymatic conversion of organic compounds, especially carbohydrates, coupling the oxidation and reduction of NAD/H and the generation of adenosine triphosphate (ATP).

The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

A membrane-bound flavoenzyme complex consisting of four subunits, A, B, C, and D. A and B comprise the membrane-extrinsic catalytic domain and C (InterPro:IPR003510; InterPro:IPR00224) and D (InterPro:IPR003418) link the catalytic centers to the electron-transport chain. In some species, the complex has only three subunits, and in these cases, there is only one membrane anchor instead of two. This family consists of the 13 kDa hydrophobic subunit D. This component may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related complex II of the respiratory chain (succinate dehydrogenase-(ubiquinone)). Examples of this component are found in bacterial species.

A membrane-bound flavoenzyme complex consisting of four subunits, A, B, C, and D. A and B comprise the membrane-extrinsic catalytic domain and C (InterPro:IPR003510; InterPro:IPR00224) and D (InterPro:IPR003418) link the catalytic centers to the electron-transport chain. In some species, the complex has only three subunits, and in these cases, there is only one membrane anchor instead of two. This family consists of the 13 kDa hydrophobic subunit D. This component may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related complex II of the respiratory chain (succinate dehydrogenase-(ubiquinone)). Examples of this component are found in bacterial species.