Allosteric enzymes as models for chemomechanical energy transducing assemblies

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

In chemomechanical energy transducing assemblies such as muscle and ATP synthase, substrates and macromolecules are locked together as partners where energy available from (or required for) a chemical transformation is exchanged with protein conformational changes. Allosteric binding proteins and enzymes are also chemomechanical energy transducers, using binding energy to generate protein conformational changes, and transduce energy in amounts almost as large as those used to drive muscle contraction and the synthesis of ATP. The recently determined structure of the F1-ATPase reveals a direct correspondence between the types of conformational changes in this transducer and simpler allosteric binding proteins and enzymes. Therefore, we can examine the structural and energetic data available on allosteric proteins to understand the linkage between ligand binding and global conformational changes in more complex energy transducing assemblies.

Original languageEnglish (US)
Pages (from-to)702-708
Number of pages7
JournalFASEB Journal
Volume10
Issue number7
StatePublished - May 1996

Fingerprint

Transducers
Muscle
energy
Carrier Proteins
Enzymes
enzymes
Adenosine Triphosphate
Proteins
H-transporting ATP synthase
Proton-Translocating ATPases
Muscle Contraction
Binding energy
Macromolecules
binding proteins
simple proteins
Ligands
Muscles
proteins
muscle contraction
Substrates

Keywords

  • ATP hydrolysis
  • conformational change
  • energy coupling
  • phosphorylation

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Allosteric enzymes as models for chemomechanical energy transducing assemblies. / Goldsmith, Elizabeth J.

In: FASEB Journal, Vol. 10, No. 7, 05.1996, p. 702-708.

Research output: Contribution to journalArticle

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