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Transport biological electron

An important enzyme in biological electron transport called cytochrome P450 gets its name from its UV absorption. The "P" stands for "pigment" because it is colored, and the "450" corresponds to the 450-nm absorption of one of its derivatives. [Pg.565]

McLendon, G. Control of Biological Electron Transport via Molecular Recognition and Binding The Velcro Model. Vol. 75, pp. 159-174. [Pg.194]

The amide functionality plays an important role in the physical and chemical properties of proteins and peptides, especially in their ability to be involved in the photoinduced electron transfer process. Polyamides and proteins are known to take part in the biological electron transport mechanism for oxidation-reduction and photosynthesis processes. Therefore studies of the photochemistry of proteins or peptides are very important. Irradiation (at 254 nm) of the simplest dipeptide, glycylglycine, in aqueous solution affords carbon dioxide, ammonia and acetamide in relatively high yields and quantum yield (0.44)202 (equation 147). The reaction mechanism is thought to involve an electron transfer process. The isolation of intermediates such as IV-hydroxymethylacetamide and 7V-glycylglycyl-methyl acetamide confirmed the electron-transfer initiated free radical processes203 (equation 148). [Pg.739]

A scries of quinones which are widely distributed in animals, plants, and microorganisms, these quinones have been shown to function in biological electron transport systems which are responsible for energy conversion with living cells. The nature and significance of coenzyme Q was first... [Pg.414]

Electrochemical studies indicate that biological cubane-type [3Fe-4S] clusters have accessible 1-F, 0, and 2— redox states. However, only the [3Fe S]+ couple appears to be used to mediate biological electron transport and redox potentials for this couple span a range from 4-90 to —460 mV (Figure 4). The midpoint potential for the two-... [Pg.2307]

The mononuclear blue (or type 1) copper proteins (cupredoxins) see Copper Proteins with Type 1 Sites), involved in biological electron transport, share a common structural motif, in which the single Cu(ll) ion is tightly bound ( 1.9-2.2 A) to two histidine and one cysteine ligand... [Pg.6343]

Bartlett, P.N. (2008) Bioenergetics and biological electron transport, in Bioelectrochemistry. Fundamentals, Experimental Techniques Ans Applications (ed. P.N. Bartlett), John Wiley Sons, Ltd, Chichester, pp. 1-38. [Pg.329]


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See also in sourсe #XX -- [ Pg.150 ]




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Biological Electron Transport Chains

Biological transporters

Electron transporter

Electron transporting

Mitochondrial electron transport biological activity

Transport biology

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