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

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

@article{f39ca9e25196474d9efae4eb3ddee5bf,

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

keywords = "Chemistry",

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

year = "2008",

month = dec,

doi = "10.1098/rsif.2008.0068.focus",

language = "English",

volume = "5",

journal = "Journal of the Royal Society Interface",

issn = "1742-5689",

publisher = "The Royal Society",

number = "SUPPL. 3",

}

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

Y1 - 2008/12

KW - Chemistry

U2 - 10.1098/rsif.2008.0068.focus

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

IS - SUPPL. 3

M1 - S225-S232

ER -