Literature DB >> 6397225

Raman study of reduced nicotinamide adenine dinucleotide bound to liver alcohol dehydrogenase.

K T Yue, J P Yang, C L Martin, S K Lee, D L Sloan, R H Callender.   

Abstract

We report the first Raman spectra of reduced nicotinamide adenine dinucleotide (NADH) when bound to an enzymatic active site, that of liver alcohol dehydrogenase (LADH). This was obtained by subtracting the Raman spectrum of LADH from that of the binary LADH/NADH complex. There are significant changes in the spectrum of bound NADH as compared to that in solution. The data indicate that both the nicotinamide moiety and the adenine moiety are involved in the binding. At least one of the two NH2 moieties of NADH also participates.

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Year:  1984        PMID: 6397225     DOI: 10.1021/bi00321a032

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  2 in total

1.  Molecular properties of pyruvate bound to lactate dehydrogenase: a Raman spectroscopic study.

Authors:  H Deng; J Zheng; J Burgner; R Callender
Journal:  Proc Natl Acad Sci U S A       Date:  1989-06       Impact factor: 11.205

2.  Hydrogen bond interactions of G proteins with the guanine ring moiety of guanine nucleotides.

Authors:  G Weng; C X Chen; V Balogh-Nair; R Callender; D Manor
Journal:  Protein Sci       Date:  1994-01       Impact factor: 6.725

  2 in total

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