Hydrogen location in stages of an enzyme-catalyzed reaction: Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose

Andrey Y. Kovalevsky; Amy K. Katz; H. L. Carrell; Leif Hanson; Marat Mustyakimov; S. Zoe Fisher; Leighton Coates; Benno P. Schoenborn; Gerard J. Bunick; Jenny P. Glusker; Paul Langan

doi:10.1021/bi8005434

Hydrogen location in stages of an enzyme-catalyzed reaction: Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose

Andrey Y. Kovalevsky, Amy K. Katz, H. L. Carrell, Leif Hanson, Marat Mustyakimov, S. Zoe Fisher, Leighton Coates, Benno P. Schoenborn, Gerard J. Bunick, Jenny P. Glusker, Paul Langan

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44 Scopus citations

Abstract

The time-of-flight neutron Laue technique has been used to determine the location of hydrogen atoms in the enzyme D-xylose isomerase (XI). The neutron structure of crystalline XI with bound product, D-xylulose, shows, unexpectedly, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated (positively charged), while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose. These findings impact our understanding of the reaction mechanism.

Original language	English
Pages (from-to)	7595-7597
Number of pages	3
Journal	Biochemistry
Volume	47
Issue number	29
DOIs	https://doi.org/10.1021/bi8005434
State	Published - Jul 22 2008
Externally published	Yes

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Kovalevsky, A. Y., Katz, A. K., Carrell, H. L., Hanson, L., Mustyakimov, M., Zoe Fisher, S., Coates, L., Schoenborn, B. P., Bunick, G. J., Glusker, J. P., & Langan, P. (2008). Hydrogen location in stages of an enzyme-catalyzed reaction: Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose. Biochemistry, 47(29), 7595-7597. https://doi.org/10.1021/bi8005434

@article{c98b78b0338b4f8a813775bc72508612,

title = "Hydrogen location in stages of an enzyme-catalyzed reaction: Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose",

abstract = "The time-of-flight neutron Laue technique has been used to determine the location of hydrogen atoms in the enzyme D-xylose isomerase (XI). The neutron structure of crystalline XI with bound product, D-xylulose, shows, unexpectedly, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated (positively charged), while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose. These findings impact our understanding of the reaction mechanism.",

author = "Kovalevsky, \{Andrey Y.\} and Katz, \{Amy K.\} and Carrell, \{H. L.\} and Leif Hanson and Marat Mustyakimov and \{Zoe Fisher\}, S. and Leighton Coates and Schoenborn, \{Benno P.\} and Bunick, \{Gerard J.\} and Glusker, \{Jenny P.\} and Paul Langan",

year = "2008",

month = jul,

day = "22",

doi = "10.1021/bi8005434",

language = "English",

volume = "47",

pages = "7595--7597",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

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}

Kovalevsky, AY, Katz, AK, Carrell, HL, Hanson, L, Mustyakimov, M, Zoe Fisher, S, Coates, L, Schoenborn, BP, Bunick, GJ, Glusker, JP & Langan, P 2008, 'Hydrogen location in stages of an enzyme-catalyzed reaction: Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose', Biochemistry, vol. 47, no. 29, pp. 7595-7597. https://doi.org/10.1021/bi8005434

TY - JOUR

T1 - Hydrogen location in stages of an enzyme-catalyzed reaction

T2 - Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose

AU - Kovalevsky, Andrey Y.

AU - Katz, Amy K.

AU - Carrell, H. L.

AU - Hanson, Leif

AU - Mustyakimov, Marat

AU - Zoe Fisher, S.

AU - Coates, Leighton

AU - Schoenborn, Benno P.

AU - Bunick, Gerard J.

AU - Glusker, Jenny P.

AU - Langan, Paul

PY - 2008/7/22

Y1 - 2008/7/22

N2 - The time-of-flight neutron Laue technique has been used to determine the location of hydrogen atoms in the enzyme D-xylose isomerase (XI). The neutron structure of crystalline XI with bound product, D-xylulose, shows, unexpectedly, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated (positively charged), while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose. These findings impact our understanding of the reaction mechanism.

AB - The time-of-flight neutron Laue technique has been used to determine the location of hydrogen atoms in the enzyme D-xylose isomerase (XI). The neutron structure of crystalline XI with bound product, D-xylulose, shows, unexpectedly, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated (positively charged), while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose. These findings impact our understanding of the reaction mechanism.

UR - https://www.scopus.com/pages/publications/47649088568

U2 - 10.1021/bi8005434

DO - 10.1021/bi8005434

M3 - Article

C2 - 18578508

AN - SCOPUS:47649088568

SN - 0006-2960

VL - 47

SP - 7595

EP - 7597

JO - Biochemistry

JF - Biochemistry

IS - 29

ER -

Hydrogen location in stages of an enzyme-catalyzed reaction: Time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose

Abstract

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