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FAD can be reduced to FADH 2 through the addition of 2 H + and 2 e −. FADH 2 can also be oxidized by the loss of 1 H + and 1 e − to form FADH. The FAD form can be recreated through the further loss of 1 H + and 1 e −. FAD formation can also occur through the reduction and dehydration of flavin-N(5)-oxide. [8]
The values below are standard apparent reduction potentials (E°') for electro-biochemical half-reactions measured at 25 °C, 1 atmosphere and a pH of 7 in aqueous solution. [1] [2] The actual physiological potential depends on the ratio of the reduced (Red) and oxidized (Ox) forms according to the Nernst equation and the thermal voltage.
Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of enzyme-catalyzed reactions. [2] Any of these may be called dehydrogenases, especially those in which NAD + is the electron acceptor (oxidant), but reductase is also used when the physiological emphasis on reduction of the substrate, and oxidase is used only when O 2 is the ...
The lighter isotope of nitrogen, 14 N, is preferred during denitrification, leaving the heavier nitrogen isotope, 15 N, in the residual matter. This selectivity leads to the enrichment of 14 N in the biomass compared to 15 N. [ 27 ] Moreover, the relative abundance of 14 N can be analyzed to distinguish denitrification apart from other ...
Abiological nitrogen fixation describes chemical processes that fix (react with) N 2, usually with the goal of generating ammonia. The dominant technology for abiological nitrogen fixation is the Haber process , which uses iron-based heterogeneous catalysts and H 2 to convert N 2 to NH 3 .
Nitrate, acting as an oxidant, is therefore reduced in a succession of four reactions performed by the enzymes nitrate, nitrite, nitric-oxide, and nitrous oxide reductases. [2] The pathway ultimately yields reduced molecular nitrogen (N 2 ), as well as, when the reaction does not reach completion, the intermediate species nitrous oxide ( N 2 O ).
Nitroreductases are a family of evolutionarily related proteins involved in the reduction of nitrogen-containing compounds, including those containing the nitro functional group. Members of this family utilise flavin mononucleotide as a cofactor and are often found to be homodimers. [1] [2]
Two protonations of the nitrogen lead to an increased N-O bond distance. The resulting intermediate is a hydroxylamine. further protonation of the hydroxylamine leads to the breakage of the N-O bond to form water. The oxidation of iron from Fe (II) to Fe (III), coupled with a further protonation of nitrogen leads to the release of ammonia.