Klaus‐Heinrich Roehm, Philipps University, Marburg, Germany
Published online: April 2001
DOI: 10.1038/npg.els.0001373
Biological electron transfer is mediated by a heterogeneous group of redox cofactors. Most of these compounds are firmly bound by proteins, others migrate freely within membranes, and some are soluble. The orderly flow of electrons through chains of such cofactors is fundamental to the generation of metabolic energy.
Keywords: redox cofactors; electron transfer; oxidative phosphorylation
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Figure 1. Overview of oxidative phosphorylation and photophosphorylation. Electron transfer steps are indicated by thin red arrows, and proton transport by thick red arrows. Dashed red arrows indicate transfer by mobile carriers. (a) Scheme of the respiratory chain; UQ/ UQH
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Figure 2. Pyridine nucleotides.
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Figure 3. Flavin cofactors.
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Figure 4. Tetrapyrrole compounds.
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Figure 5. Iron–sulfur clusters.
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Figure 6. Quinones.
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| Further Reading | |
| Beinert H, Holm RH and Münck E (1997) Iron–sulfur clusters: Nature's modular, multipurpose structures. Science 277: 653–659. | |
| Gray HB and Winkler JR (1996) Electron transfer in proteins. Annual Review of Biochemistry 65: 537–561. | |
| Nugent JH (1996) Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II. European Journal of Biochemistry 237: 519–531. | |
| Saraste M (1999) Oxidative phosphorylation at the fin des siècle. Science 283: 1488–1493. | |
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