Abstract
Electron transfer cofactors are non-protein molecules that bind to proteins and enzymes and act as conduits for the passage of electrons in redox reactions.
Life in all organisms relies on electron transport to facilitate molecular transformations and for fundamental processes such as respiration and photosynthesis. These reactions are described by electron transfer theory. Biological electron transfer reactions are performed predominantly by proteins and generally rely on the presence of cofactors: non-proteinaceous molecules bound to proteins and enzymes that enable their biological functions. The cofactors may be organic molecules such as flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), nicotinamide adenine dinucleotide (NADH), and quinone cofactors. The cofactors may be inorganic, such as iron–sulfur clusters, or organometallic such as hemes. These cofactors are components of respiratory and photosynthetic electron...
Life in all organisms relies on electron transport to facilitate molecular transformations and for fundamental processes such as respiration and photosynthesis. These reactions are described by electron transfer theory. Biological electron transfer reactions are performed predominantly by proteins and generally rely on the presence of cofactors: non-proteinaceous molecules bound to proteins and enzymes that enable their biological functions. The cofactors may be organic molecules such as flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), nicotinamide adenine dinucleotide (NADH), and quinone cofactors. The cofactors may be inorganic, such as iron–sulfur clusters, or organometallic such as hemes. These cofactors are components of respiratory and photosynthetic electron...
| Original language | English |
|---|---|
| Title of host publication | Encyclopedia of Biophysics |
| Editors | Gordon C. K. Roberts |
| Publisher | Springer |
| Pages | 601-606 |
| Number of pages | 6 |
| Edition | 1st |
| ISBN (Electronic) | 9783642167126 |
| ISBN (Print) | 9783642167119 |
| DOIs | |
| Publication status | Published - 8 Oct 2012 |
| Externally published | Yes |
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