Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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...
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...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Mechanism of Photoinduced Conformational Changes in the Photoenzyme Fatty Acid Photodecarboxylase Revealed by Light- Footprinting Ion Mobility Mass Spectrometry.

Journal of the American Chemical Society·2026
Same author

Bromazolam Tablet Quantification and Analysis of Post-Mortem Cases From the National Programme on Substance Use Mortality (NPSUM).

Drug testing and analysis·2026
Same author

Environmental Dipolar Relaxation during Excited-State Proton Transfer in Green Fluorescent Protein.

Journal of the American Chemical Society·2026
Same author

Integrated structural dynamics uncover a new B<sub>12</sub> photoreceptor activation mode.

Nature·2026
Same author

Optimising environmental factors for maximal lactate productivity in Synechocystis sp. PCC 6803 through a design of experiments approach.

Biotechnology for biofuels and bioproducts·2025
Same author

Expanding the substrate scope of a bacterial monoterpene synthase for the production of sesquiterpenoid and diterpenoid products.

The FEBS journal·2025

関連する実験動画

Updated: May 14, 2026

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
05:51

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method

Published on: July 19, 2019

酵素による単一分子動的同位体効果

Christopher R Pudney1, Richard S K Lane, Alistair J Fielding

  • 1Manchester Institute of Biotechnology and Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.

Journal of the American Chemical Society
|February 14, 2013
PubMed
まとめ

spFRETを使用した単一分子運動同位体効果 (KIEs) は,酵素反応の詳細を明らかにします. この方法では,酵素によるH転送をタンパク質とフッ素ホルダーダイナミクスから分離し,触媒の理解を深める.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 酵素の動力学について
  • 物理化学 物理化学とは

背景:

  • キネティック・イソトープ効果 (KIEs) の総合的な測定は,酵素触媒反応の理解を深めたが,限界に直面している.
  • KIEsは,速度制限ステップ,量子トンネル,ダイナミクス,および酵素の複数の反応状態の研究に不可欠です.

研究 の 目的:

  • 酵素触媒に関する新しい洞察を得るために単一分子 (SM) 酵素KIEを探求する.
  • 単一ペアの光エネルギー伝送 (spFRET) を適用して,H伝送反応におけるKIEを測定する.

主な方法:

  • 単一ペアの光エネルギー伝送 (spFRET) を利用して,SME KIEsを測定しました.
  • spFRETのタイムトラッキングからSME KIEsを抽出するための方法を開発し,評価しました.
  • ペンタエリトリトールテトランニートレドゥクタゼによって触媒化された研究されたH-トランスファー.

主要な成果:

  • H転送反応のためのSM酵素KIEを測定しました.
  • SM KIE分析の酵素と非酵素のプロセスを区別する能力を実証しました.
  • タンパク質のダイナミクス,フッ素ホルダーの行動,およびH-転送反応自体の分離された貢献.

さらに関連する動画

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

関連する実験動画

Last Updated: May 14, 2026

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
05:51

Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method

Published on: July 19, 2019

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

結論:

  • 単一分子KIE分析は,酵素触媒を研究するための強力な新しいアプローチを提供します.
  • この方法は,タンパク質の固有動力学から反応化学の解消を可能にします.
  • 酵素動力学における長年の論争を解決する道を提示する.