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An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.
This functionality is used in cytochromes, which function as electron-transfer vectors. The presence of the metal ion allows metalloenzymes to perform functions such as redox reactions that cannot easily be performed by the limited set of functional groups found in amino acids. [16] The iron atom in most cytochromes is contained in a heme group ...
The P450 systems that are located in the mitochondria are dependent on two electron transfer proteins: An FAD containing adrenodoxin reductase (AR) and a small iron-sulfur group containing protein named adrenodoxin. FAD is embedded in the FAD-binding domain of AR.
Hemeproteins also enable electron transfer as they form part of the electron transport chain. Cytochrome a, cytochrome b, and cytochrome c have such electron transfer functions. It is now known that cytochrome a and cytochrome a3 make up one protein and was deemed the name cytochrome aa3. [8]
The blue copper protein often called as "moonlighting protein", which means a protein can perform more than one function. They serve as electron transfer agents, with the active site shuttling between Cu(I) and Cu(II). The Cu 2+ in the oxidized state can accept one electron to form Cu 1+ in the reduced protein. The geometry of the Cu center has ...
An electron transfer flavoprotein (ETF) or electron transfer flavoprotein complex (CETF) is a flavoprotein located on the matrix face of the inner mitochondrial membrane and functions as a specific electron acceptor for primary dehydrogenases, transferring the electrons to terminal respiratory systems such as electron-transferring-flavoprotein dehydrogenase.
Transport of the positively charged proton is typically electrogenic, i.e.: it generates an electric field across the membrane also called the membrane potential.Proton transport becomes electrogenic if not neutralized electrically by transport of either a corresponding negative charge in the same direction or a corresponding positive charge in the opposite direction.
The [Fe 4 S 4] electron-transfer proteins ([Fe 4 S 4] ferredoxins) may be further subdivided into low-potential (bacterial-type) and high-potential (HiPIP) ferredoxins. Low- and high-potential ferredoxins are related by the following redox scheme: 4Fe-4S clusters serve as electron-relays in proteins.