Protein recognition of ammonium cations using side-chain aromatics: A structural variation for secondary ammonium ligands

A. R C Raine; C. C. Yang; L. C. Packman; S. A. White; F. S. Mathews; N. S. Scrutton

Protein recognition of ammonium cations using side-chain aromatics: A structural variation for secondary ammonium ligands

A. R C Raine, C. C. Yang, L. C. Packman, S. A. White, F. S. Mathews, N. S. Scrutton

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

Abstract

A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-π bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-π and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.

Original language	English
Pages (from-to)	2625-2628
Number of pages	3
Journal	Protein science
Volume	4
Issue number	12
Publication status	Published - 1995

Keywords

ammonium ligands
flavoprotein
methylamine dehydrogenases
organic cation-π bonding

Cite this

@article{86c00743633540efa03b2f3fb34a6bdf,

title = "Protein recognition of ammonium cations using side-chain aromatics: A structural variation for secondary ammonium ligands",

abstract = "A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-π bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-π and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.",

keywords = "ammonium ligands, flavoprotein, methylamine dehydrogenases, organic cation-π bonding",

author = "Raine, {A. R C} and Yang, {C. C.} and Packman, {L. C.} and White, {S. A.} and Mathews, {F. S.} and Scrutton, {N. S.}",

year = "1995",

language = "English",

volume = "4",

pages = "2625--2628",

journal = "Protein science",

issn = "0961-8368",

publisher = "Cold Spring Harbor Laboratory Press",

number = "12",

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TY - JOUR

T1 - Protein recognition of ammonium cations using side-chain aromatics: A structural variation for secondary ammonium ligands

AU - Raine, A. R C

AU - Yang, C. C.

AU - Packman, L. C.

AU - White, S. A.

AU - Mathews, F. S.

AU - Scrutton, N. S.

PY - 1995

Y1 - 1995

N2 - A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-π bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-π and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.

AB - A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-π bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-π and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.

KW - ammonium ligands

KW - flavoprotein

KW - methylamine dehydrogenases

KW - organic cation-π bonding

M3 - Article

SN - 0961-8368

VL - 4

SP - 2625

EP - 2628

JO - Protein science

JF - Protein science

IS - 12

ER -

Protein recognition of ammonium cations using side-chain aromatics: A structural variation for secondary ammonium ligands

Abstract

Keywords

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