Hydrogen bonding and reaction specificity in lactate dehydrogenase studied by Raman spectroscopy

Hua Deng, Jie Zheng, John Burgner, Robert Callender

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The Raman spectrum of a small molecule or molecular moiety when bound to sizable proteins can be measured by using difference techniques developed in our laboratory. We have applied this method in obtaining the Raman spectrum of the cofactor acetylpyridine adenine dinucleotide, APAD+, when bound to lactate dehydrogenase. The Raman data permit a characterization of some of the molecular interactions responsible for the stereochemistry of the reaction catalyzed by this enzyme. We find that the enzyme forms a strong hydrogen bond with the cofactor's carboxamide group and suggest that this is at least partially responsible for the very high degree of stereochemistry fidelity observed with this enzyme.

Original languageEnglish (US)
Pages (from-to)4710-4713
Number of pages4
JournalJournal of Physical Chemistry
Volume93
Issue number12
StatePublished - 1989
Externally publishedYes

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lactates
dehydrogenases
L-Lactate Dehydrogenase
Raman spectroscopy
enzymes
Hydrogen bonds
Stereochemistry
Enzymes
stereochemistry
Raman scattering
hydrogen
Raman spectra
Molecular interactions
adenines
Adenine
molecular interactions
hydrogen bonds
proteins
Proteins
Molecules

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Hydrogen bonding and reaction specificity in lactate dehydrogenase studied by Raman spectroscopy. / Deng, Hua; Zheng, Jie; Burgner, John; Callender, Robert.

In: Journal of Physical Chemistry, Vol. 93, No. 12, 1989, p. 4710-4713.

Research output: Contribution to journalArticle

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