Standard

NMR localization of protons in critical enzyme hydrogen bonds. / Sharif, Shasad; Fogle, Emily; Toney, Michael D.; Denisov, Gleb S.; Shenderovich, Ilya G.; Buntkowsky, Gerd; Tolstoy, Peter M.; Huot, Monique Chan; Limbach, Hans Heinrich.

In: Journal of the American Chemical Society, Vol. 129, No. 31, 08.08.2007, p. 9558-9559.

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

Harvard

Sharif, S, Fogle, E, Toney, MD, Denisov, GS, Shenderovich, IG, Buntkowsky, G, Tolstoy, PM, Huot, MC & Limbach, HH 2007, 'NMR localization of protons in critical enzyme hydrogen bonds', Journal of the American Chemical Society, vol. 129, no. 31, pp. 9558-9559. https://doi.org/10.1021/ja0728223

APA

Sharif, S., Fogle, E., Toney, M. D., Denisov, G. S., Shenderovich, I. G., Buntkowsky, G., Tolstoy, P. M., Huot, M. C., & Limbach, H. H. (2007). NMR localization of protons in critical enzyme hydrogen bonds. Journal of the American Chemical Society, 129(31), 9558-9559. https://doi.org/10.1021/ja0728223

Vancouver

Sharif S, Fogle E, Toney MD, Denisov GS, Shenderovich IG, Buntkowsky G et al. NMR localization of protons in critical enzyme hydrogen bonds. Journal of the American Chemical Society. 2007 Aug 8;129(31):9558-9559. https://doi.org/10.1021/ja0728223

Author

Sharif, Shasad ; Fogle, Emily ; Toney, Michael D. ; Denisov, Gleb S. ; Shenderovich, Ilya G. ; Buntkowsky, Gerd ; Tolstoy, Peter M. ; Huot, Monique Chan ; Limbach, Hans Heinrich. / NMR localization of protons in critical enzyme hydrogen bonds. In: Journal of the American Chemical Society. 2007 ; Vol. 129, No. 31. pp. 9558-9559.

BibTeX

@article{0ddf95ad5f42420c825bb7105f6f235e,
title = "NMR localization of protons in critical enzyme hydrogen bonds",
abstract = "Using 15N NMR spectroscopy and hydrogen bond correlations, we have localized a mechanistically critical proton in aspartate aminotransferase in microcrystals and aqueous solution. It is in a H-bond between a carboxylate O of Asp222 and the pyridine nitrogen of pyridoxal-5′-phosphate. At neutral pH in water, aspartate and pyridine are unprotonated, but they share a proton in the enzyme. It is shown that such a binuclear base is typical for acid-base interactions in aprotic polar solvents. Active site H-bonds to Asp222 assist protonation of the pyridine nitrogen in the enzyme, which is considered a prerequisite for catalytic activity. We also show that acid-base behavior in enzymes should be modeled using aprotic polar solvents rather than aqueous solutions.",
author = "Shasad Sharif and Emily Fogle and Toney, {Michael D.} and Denisov, {Gleb S.} and Shenderovich, {Ilya G.} and Gerd Buntkowsky and Tolstoy, {Peter M.} and Huot, {Monique Chan} and Limbach, {Hans Heinrich}",
year = "2007",
month = aug,
day = "8",
doi = "10.1021/ja0728223",
language = "English",
volume = "129",
pages = "9558--9559",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "31",

}

RIS

TY - JOUR

T1 - NMR localization of protons in critical enzyme hydrogen bonds

AU - Sharif, Shasad

AU - Fogle, Emily

AU - Toney, Michael D.

AU - Denisov, Gleb S.

AU - Shenderovich, Ilya G.

AU - Buntkowsky, Gerd

AU - Tolstoy, Peter M.

AU - Huot, Monique Chan

AU - Limbach, Hans Heinrich

PY - 2007/8/8

Y1 - 2007/8/8

N2 - Using 15N NMR spectroscopy and hydrogen bond correlations, we have localized a mechanistically critical proton in aspartate aminotransferase in microcrystals and aqueous solution. It is in a H-bond between a carboxylate O of Asp222 and the pyridine nitrogen of pyridoxal-5′-phosphate. At neutral pH in water, aspartate and pyridine are unprotonated, but they share a proton in the enzyme. It is shown that such a binuclear base is typical for acid-base interactions in aprotic polar solvents. Active site H-bonds to Asp222 assist protonation of the pyridine nitrogen in the enzyme, which is considered a prerequisite for catalytic activity. We also show that acid-base behavior in enzymes should be modeled using aprotic polar solvents rather than aqueous solutions.

AB - Using 15N NMR spectroscopy and hydrogen bond correlations, we have localized a mechanistically critical proton in aspartate aminotransferase in microcrystals and aqueous solution. It is in a H-bond between a carboxylate O of Asp222 and the pyridine nitrogen of pyridoxal-5′-phosphate. At neutral pH in water, aspartate and pyridine are unprotonated, but they share a proton in the enzyme. It is shown that such a binuclear base is typical for acid-base interactions in aprotic polar solvents. Active site H-bonds to Asp222 assist protonation of the pyridine nitrogen in the enzyme, which is considered a prerequisite for catalytic activity. We also show that acid-base behavior in enzymes should be modeled using aprotic polar solvents rather than aqueous solutions.

UR - http://www.scopus.com/inward/record.url?scp=34547738664&partnerID=8YFLogxK

U2 - 10.1021/ja0728223

DO - 10.1021/ja0728223

M3 - Article

C2 - 17628065

AN - SCOPUS:34547738664

VL - 129

SP - 9558

EP - 9559

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 31

ER -

ID: 100705154