The hydride-donation reaction of reduced nicotinamide adenine dinucleotide. 2. MINDO/3 and STO-3G calculations on the role of the carbamoyl group in enzymic reactions

M.C.A. Donkersloot; H.M. Buck

doi:10.1021/ja00412a003

The hydride-donation reaction of reduced nicotinamide adenine dinucleotide. 2. MINDO/3 and STO-3G calculations on the role of the carbamoyl group in enzymic reactions

M.C.A. Donkersloot, H.M. Buck

Chemical Engineering and Chemistry

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Abstract

The enzyme-catalyzed stereospecific hydride-transfer equilibrium RH + NAD’ R+ + NADH has been studied with the help of semiempirical (MIND0/3) and ab initio (STO-3Gc)a lculations on corresponding model compounds. It seems possible to relate the stereospecificity simply to an out-of-plane orientation of the CONH2 group in the transition state of the reaction. One of the important functions of the enzyme would be to freeze the otherwise almost freely rotating CONHz group in a favorable orientation.

Original language	English
Pages (from-to)	6554-6558
Journal	Journal of the American Chemical Society
Volume	103
Issue number	22
DOIs	https://doi.org/10.1021/ja00412a003
Publication status	Published - 1981

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abstract = "The enzyme-catalyzed stereospecific hydride-transfer equilibrium RH + NAD{\textquoteright} R+ + NADH has been studied with the help of semiempirical (MIND0/3) and ab initio (STO-3Gc)a lculations on corresponding model compounds. It seems possible to relate the stereospecificity simply to an out-of-plane orientation of the CONH2 group in the transition state of the reaction. One of the important functions of the enzyme would be to freeze the otherwise almost freely rotating CONHz group in a favorable orientation.",

author = "M.C.A. Donkersloot and H.M. Buck",

year = "1981",

doi = "10.1021/ja00412a003",

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journal = "Journal of the American Chemical Society",

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publisher = "American Chemical Society",

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AU - Donkersloot, M.C.A.

AU - Buck, H.M.

PY - 1981

Y1 - 1981

N2 - The enzyme-catalyzed stereospecific hydride-transfer equilibrium RH + NAD’ R+ + NADH has been studied with the help of semiempirical (MIND0/3) and ab initio (STO-3Gc)a lculations on corresponding model compounds. It seems possible to relate the stereospecificity simply to an out-of-plane orientation of the CONH2 group in the transition state of the reaction. One of the important functions of the enzyme would be to freeze the otherwise almost freely rotating CONHz group in a favorable orientation.

AB - The enzyme-catalyzed stereospecific hydride-transfer equilibrium RH + NAD’ R+ + NADH has been studied with the help of semiempirical (MIND0/3) and ab initio (STO-3Gc)a lculations on corresponding model compounds. It seems possible to relate the stereospecificity simply to an out-of-plane orientation of the CONH2 group in the transition state of the reaction. One of the important functions of the enzyme would be to freeze the otherwise almost freely rotating CONHz group in a favorable orientation.

U2 - 10.1021/ja00412a003

DO - 10.1021/ja00412a003

M3 - Article

SN - 0002-7863

VL - 103

SP - 6554

EP - 6558

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 22

ER -

The hydride-donation reaction of reduced nicotinamide adenine dinucleotide. 2. MINDO/3 and STO-3G calculations on the role of the carbamoyl group in enzymic reactions

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