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Updated: Aug 4, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
05:51

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase

Published on: December 19, 2011

中鎖アシル-コア脱水素酵素の活性部位におけるリング電流効果は,NMRスペクトロスコピーによって明らかになった

Jiaquan Wu1, Alasdair F Bell, Andrew A Jaye

  • 1Department of Chemistry, Stony Brook University, Stony Brook, NY 11794-3400, USA.

Journal of the American Chemical Society
|June 9, 2005
PubMed
まとめ

核磁共振 (NMR) とラーマン光譜法では,ヘキサディエノイル-CoA (HD-CoA) と酵素の間の明確な相互作用が明らかにされています. フラビン共因子 (flavin cofactor) が含まれる.

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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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IR and UV–Vis Spectroscopy of Carboxylic Acids

In IR spectroscopy of carboxylic acids, the C=O bond shows a characteristic band between 1710 and 1760 cm⁻¹, and the O–H bond exhibits a broad band between 2500 and 3300 cm⁻¹.
However, the stretching absorptions for the C=O bond vary depending on the structure of carboxylic acids. The C=O bond of the free carboxylic acids shows a higher stretching frequency, 1760 cm−1, while H-bonded carboxylic acids (dimers) exhibit stretching absorptions at a lower frequency, 1710 cm−1. The C=O bond of the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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NMR and Mass Spectroscopy of Carboxylic Acids

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While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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