Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

L. Chen; F.S. Mathews; V.L. Davidson; E.G. Huizinga; F.M.D. Vellieux; J.A. Duine; W.G.J. Hol

doi:10.1016/0014-5793(91)80041-Z

Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

L. Chen, F.S. Mathews, V.L. Davidson, E.G. Huizinga, F.M.D. Vellieux, J.A. Duine, W.G.J. Hol

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

Abstract

A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.

Original language	English
Pages (from-to)	163-166
Number of pages	4
Journal	FEBS Letters
Volume	287
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(91)80041-Z
Publication status	Published - 22 Dec 1991
Externally published	Yes

Keywords

amino acid-derived cofactor
methylamine dehydrogenase
pyrroloquinoline quinone
quinoprotein
redox cofactor
tryptophan tryptophylquinone
amine dehydrogenase
article
chemical structure
controlled study
crystallography
priority journal

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10.1016/0014-5793(91)80041-Z

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title = "Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase",

abstract = "A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.",

keywords = "amino acid-derived cofactor, methylamine dehydrogenase, pyrroloquinoline quinone, quinoprotein, redox cofactor, tryptophan tryptophylquinone, amine dehydrogenase, article, chemical structure, controlled study, crystallography, priority journal",

author = "L. Chen and F.S. Mathews and V.L. Davidson and E.G. Huizinga and F.M.D. Vellieux and J.A. Duine and W.G.J. Hol",

year = "1991",

month = dec,

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doi = "10.1016/0014-5793(91)80041-Z",

language = "English",

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journal = "FEBS Letters",

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T1 - Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

AU - Chen, L.

AU - Mathews, F.S.

AU - Davidson, V.L.

AU - Huizinga, E.G.

AU - Vellieux, F.M.D.

AU - Duine, J.A.

AU - Hol, W.G.J.

PY - 1991/12/22

Y1 - 1991/12/22

N2 - A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.

AB - A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.

KW - amino acid-derived cofactor

KW - methylamine dehydrogenase

KW - pyrroloquinoline quinone

KW - quinoprotein

KW - redox cofactor

KW - tryptophan tryptophylquinone

KW - amine dehydrogenase

KW - article

KW - chemical structure

KW - controlled study

KW - crystallography

KW - priority journal

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DO - 10.1016/0014-5793(91)80041-Z

M3 - Article

SN - 0014-5793

VL - 287

SP - 163

EP - 166

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

Abstract

Keywords

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