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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
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The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
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Introduction to Enzyme Kinetics01:19

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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Characterizing Electron Transport through Living Biofilms
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Diameter dependent electron transfer kinetics in semiconductor-enzyme complexes.

Katherine A Brown1, Qing Song, David W Mulder

  • 1Biosciences Center, National Renewable Energy Laboratory , Golden, Colorado 80401, United States.

ACS Nano
|September 23, 2014
PubMed
Summary
This summary is machine-generated.

Electron transfer kinetics between quantum dots and enzymes are key for solar energy conversion. This study found that enzyme surface coverage, not just energy levels, dictates electron transfer rates and catalytic efficiency.

Keywords:
binding complexbiohybridhydrogeninterfacial electron-transfernanoparticlephotochemical

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Area of Science:

  • Photocatalysis
  • Nanomaterials Science
  • Biocatalysis

Background:

  • Excited state electron transfer (ET) is crucial for converting solar energy to chemical energy.
  • Understanding ET kinetics between photoexcited nanoparticles and catalysts is vital for optimizing solar energy applications.
  • Cadmium telluride (CdTe) quantum dots and [FeFe]-hydrogenase I (CaI) are model systems for studying these processes.

Purpose of the Study:

  • To investigate the factors controlling electron transfer (ET) kinetics between photoexcited CdTe quantum dots and Clostridium acetobutylicum [FeFe]-hydrogenase I (CaI).
  • To determine the influence of nanoparticle size and enzyme surface coverage on ET rates and catalytic turnover frequency (TOF).

Main Methods:

  • Utilized time-resolved photoluminescence spectroscopy to measure ET kinetics in solution-phase CdTe quantum dot and CaI complexes.
  • Employed Langmuir isotherm and geometric binding models to estimate CaI binding affinities and surface coverages on CdTe nanoparticles of varying diameters (2.0-3.5 nm).
  • Measured the turnover frequency (TOF) of CaI in CdTe-CaI complexes across different molar ratios.

Main Results:

  • Observed that ET rate (kET) was initially sensitive to CaI concentration but became insensitive to CdTe diameter upon normalization to CaI surface coverage.
  • Found that normalized kET values remained constant despite a decrease in the free energy for photoexcited ET (ΔGET) with increasing CdTe diameter.
  • Demonstrated that normalized turnover frequency (TOF) increased with CdTe diameter, indicating enhanced catalytic activity.

Conclusions:

  • ET kinetics and H2 production in CdTe-CaI complexes are not solely governed by the free energy of electron transfer (ΔGET).
  • Enzyme surface coverage plays a critical role in modulating both electron transfer efficiency and catalytic performance.
  • These findings highlight the importance of considering geometric and surface effects beyond thermodynamic driving forces in designing artificial photosynthetic systems.