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Related Concept Videos

Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Introduction to Enzymes01:22

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...

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Related Experiment Video

Updated: Jun 26, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

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Published on: May 29, 2011

Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.

Olga A Sytina1, Derren J Heyes, C Neil Hunter

  • 1Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands.

Nature
|December 19, 2008
PubMed
Summary

Enzyme conformational changes, crucial for catalytic power, were elucidated using NADPH:protochlorophyllide oxidoreductase. Laser excitation induced favorable active site conformations, enabling efficient hydride and proton transfers for catalysis.

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Enzyme catalytic power is a major biological question.
  • Enzymes modulate reaction rates via protein motions, but distinguishing this from catalysis is difficult.

Purpose of the Study:

  • To investigate the role of conformational changes in enzyme catalysis.
  • To use NADPH:protochlorophyllide (Pchlide) oxidoreductase as a model system for a light-driven reaction.

Main Methods:

  • Studied the chlorophyll biosynthetic enzyme NADPH:protochlorophyllide (Pchlide) oxidoreductase.
  • Utilized laser pulse excitation of the enzyme-substrate complex.
  • Analyzed spectral changes using mid-infrared spectroscopy following single-photon absorption.

Main Results:

  • Laser excitation induced a more favorable enzyme active site conformation.
  • This conformational change enabled coupled hydride and proton transfer reactions.
  • Observed spectral changes indicated significant enzyme conformational changes and dynamics.

Conclusions:

  • Conformational changes are critical for enzyme catalytic efficiency.
  • Enzyme flexibility and dynamics are essential for function.
  • Light-induced conformational changes can switch enzymes into a highly active state.