Raman Study of Reduced Nicotinamide Adenine Dinucleotide Bound to Liver Alcohol Dehydrogenase

Kwok To Yue; Jing Peng Yang; Shun K. Lee; Robert H. Callender; Charlotte L. Martin; Donald L. Sloan

doi:10.1021/bi00321a032

Raman Study of Reduced Nicotinamide Adenine Dinucleotide Bound to Liver Alcohol Dehydrogenase

Kwok To Yue, Jing Peng Yang, Shun K. Lee, Robert H. Callender, Charlotte L. Martin, Donald L. Sloan

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

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.

Original language	English (US)
Pages (from-to)	6480-6483
Number of pages	4
Journal	Biochemistry
Volume	23
Issue number	26
DOIs	https://doi.org/10.1021/bi00321a032
State	Published - Dec 1984
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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title = "Raman Study of Reduced Nicotinamide Adenine Dinucleotide Bound to Liver Alcohol Dehydrogenase",

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.",

author = "Yue, {Kwok To} and Yang, {Jing Peng} and Lee, {Shun K.} and Callender, {Robert H.} and Martin, {Charlotte L.} and Sloan, {Donald L.}",

year = "1984",

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doi = "10.1021/bi00321a032",

language = "English (US)",

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pages = "6480--6483",

journal = "Biochemistry",

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publisher = "American Chemical Society",

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T1 - Raman Study of Reduced Nicotinamide Adenine Dinucleotide Bound to Liver Alcohol Dehydrogenase

AU - Yue, Kwok To

AU - Yang, Jing Peng

AU - Lee, Shun K.

AU - Callender, Robert H.

AU - Martin, Charlotte L.

AU - Sloan, Donald L.

PY - 1984/12

Y1 - 1984/12

N2 - 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.

AB - 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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AN - SCOPUS:0021766671

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SP - 6480

EP - 6483

JO - Biochemistry

JF - Biochemistry

IS - 26

ER -

Raman Study of Reduced Nicotinamide Adenine Dinucleotide Bound to Liver Alcohol Dehydrogenase

Abstract

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