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The microbes in a MFC may gain all the energy and carbon required for cellular growth from the oxidation of the complex organic material and as such MFC technology has been considered self-sustaining [7].
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Fewer ATP molecules result from the oxidation of FADH2 as complex II does not translocate any protons.
This stems from the work of two independent research groups who reported that metformin selectively inhibits the oxidation of complex I substrates but not complex II or IV substrates [ 10, 12].
Peroxide is also produced from the oxidation of reduced flavoproteins, such as complex I.
In parallel to the proton movement, the electrons that were produced from the oxidation of NADH are transported through complexes I and III and then bind oxygen to generate water at complex IV.
Δψm is generated by a series of four protein complexes (complex I-IV, respectively) in the mitochondrial inner membrane, which transfer electrons derived from the oxidation of reduced nicotinamide adenine dinucleotide (NADH) by complex I (NADH-ubiquinone oxidoreductase) or from the oxidation of succinate by complex II (succinate-ubiquinone oxidoreductase).
The small change in the rates of the oxidation of iminodiacetatochromium III) complexes (Table 5) are shown to arise from parallel changes ΔH* and ΔS*.
The OXPHOS machinery consists of four enzyme complexes in the respiratory chain that transport electrons obtained from the oxidation of carbohydrates and fats to molecular oxygen (O2); a fifth enzyme complex uses the energy derived from this process to drive ATP synthesis.
Thus, the production of ATP from the oxidation of pyruvate to acetate is unlikely, given that the pyruvate dehydrogenase complex and the acetate kinase are missing.
We assayed Complex IV activity spectrophotometrically by the decrease in absorbance at 550 nm resulting from the oxidation of pre-reduced cytochrome c.
Complex IV activity assay was performed following the decrease in absorbance at 550 nm resulting from the oxidation of reduced cytochrome c.
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