The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer

Linus, O. Johannissen; Nigel, S. Scrutton; Michael, J. Sutcliffe

doi:10.1098/rsif.2008.0068.focus

The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer

Linus, O. Johannissen, Nigel, S. Scrutton, Michael, J. Sutcliffe

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

Original language	English
Article number	S225-S232
Journal	Journal of the Royal Society Interface
Volume	5
Issue number	SUPPL. 3
DOIs	https://doi.org/10.1098/rsif.2008.0068.focus
Publication status	Published - Dec 2008
Externally published	Yes

Keywords

Chemistry

Access to Document

10.1098/rsif.2008.0068.focus

http://dx.doi.org/10.1098/rsif.2008.0068.focus

Cite this

Johannissen, L. O., Scrutton, N. S., & Sutcliffe, M. J. (2008). The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer. Journal of the Royal Society Interface, 5(SUPPL. 3), Article S225-S232. https://doi.org/10.1098/rsif.2008.0068.focus

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author = "Johannissen, \{Linus, O.\} and Scrutton, \{Nigel, S.\} and Sutcliffe, \{Michael, J.\}",

year = "2008",

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language = "English",

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The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer. / Johannissen, Linus, O.; Scrutton, Nigel, S.; Sutcliffe, Michael, J.
In: Journal of the Royal Society Interface, Vol. 5, No. SUPPL. 3, S225-S232, 12.2008.

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

TY - JOUR

T1 - The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer

AU - Johannissen, Linus, O.

AU - Scrutton, Nigel, S.

AU - Sutcliffe, Michael, J.

PY - 2008/12

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KW - Chemistry

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DO - 10.1098/rsif.2008.0068.focus

M3 - Article

SN - 1742-5689

VL - 5

JO - Journal of the Royal Society Interface

JF - Journal of the Royal Society Interface

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