Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Limei Hsu Jones"'
Publikováno v:
Biochemistry. 45:13276-13283
Tryptophan tryptophylquinone (TTQ), the prosthetic group of methylamine dehydrogenase, is formed by post-translational modifications of two tryptophan residues that result in the incorporation of two oxygens into one tryptophan side chain and the cov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b88d72bdc1e897010305cfcb276b71fc
https://doi.org/10.1021/bi061497d
https://doi.org/10.1021/bi061497d
Autor:
Arwen R. Pearson, Paul A. Grimsrud, Sudha Marimanikkupam, M. Elizabeth Graichen, Sean A. Agger, Carrie M. Wilmot, Limei Hsu Jones, Yongting Wang, Teresa De la Mora-Rey, Victor L. Davidson
Publikováno v:
Biochemistry. 43:5494-5502
Paracoccus denitrificans methylamine dehydrogenase (MADH) is an enzyme containing a quinone cofactor tryptophan tryptophylquinone (TTQ) derived from two tryptophan residues (betaTrp(57) and betaTrp(108)) within the polypeptide chain. During cofactor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ee889935ac13d5c94ebe895ec6809da
https://doi.org/10.1021/bi049863l
https://doi.org/10.1021/bi049863l
Publikováno v:
Journal of Biological Chemistry. 278:47269-47274
The type I copper center of amicyanin was replaced with a binuclear CuA center. To create this model CuA protein, a portion of the amino acid sequence that contains three of the ligands to the native type I copper center of Paracoccus denitrificans a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa4837ff4ecf7dafdb7e285a8d936e89
https://doi.org/10.1074/jbc.m308863200
https://doi.org/10.1074/jbc.m308863200
Autor:
LeeAnn Higgins, Victor L. Davidson, Arwen R. Pearson, Alison E. Ashcroft, Limei Hsu Jones, Carrie M. Wilmot
Publikováno v:
Biochemistry. 42:3224-3230
Cofactors made from constitutive amino acids in proteins are now known to be relatively common. A number of these involve the generation of quinone cofactors, such as topaquinone in the copper-containing amine oxidases, and lysine tyrosylquinone in l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72f6dc4e8f3336da2a048ba07593efd0
https://doi.org/10.1021/bi027073a
https://doi.org/10.1021/bi027073a
Publikováno v:
Protein Engineering, Design and Selection. 14:675-681
Site-directed mutagenesis was used to alter active-site residues of methylamine dehydrogenase (MADH) from Paracoccus denitrificans. Four residues of the beta subunit of MADH which are in close proximity to the tryptophan tryptophylquinone (TTQ) prost
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3580fbb7f06aba9bce10196a4b49d09d
https://doi.org/10.1093/protein/14.9.675
https://doi.org/10.1093/protein/14.9.675
Publikováno v:
Biochemistry. 39:8830-8836
Methylamine dehydrogenase (MADH) and amicyanin form a physiologic complex which is required for interprotein electron transfer. The crystal structure of this protein complex is known, and the importance of certain residues on amicyanin in its interac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a88db5d25ff7f95cae23171106da9ca
https://doi.org/10.1021/bi000502p
https://doi.org/10.1021/bi000502p
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1457(1-2):27-35
A Pathways analysis of the methylamine dehydrogenase–amicyanin–cytochrome c -551i protein electron transfer (ET) complex predicts two sets of ET pathways of comparable efficiency from the type I copper of amicyanin to the heme of cytochrome c -55
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f85620aa27ee9eb74e59c5f295733cfe
Publikováno v:
Biochemistry. 37:7371-7377
Conversion by site-directed mutagenesis of Phe 97 of amicyanin to Glu significantly decreases the rate constant for the electron-transfer reaction from the quinol form of methylamine dehydrogenase to amicyanin. It is shown that the DeltaG degrees and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b78d4e7fc2a2783443c8b9eb02ee63f
https://doi.org/10.1021/bi973020v
https://doi.org/10.1021/bi973020v
Autor:
F. S. Mathews, Pappannan Thiyagarajan, Limei Hsu Jones, Paul Langan, Narayanasami Sukumar, Benno P. Schoenborn, Victor L. Davidson
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 61:640-642
Crystals of the blue copper protein amicyanin suitable for neutron diffraction were grown by the sitting-drop method, followed by repeated macroseeding using solutions prepared with D{sub 2}O. Although the crystal sizes were the same, crystals grown
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a678e564f1318734231e7471fb28e2cd
https://doi.org/10.1107/s090744490500541x
https://doi.org/10.1107/s090744490500541x
Autor:
Victor L. Davidson, Limei Hsu Jones
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1252:146-150
Phenylhydrazine has previously been shown to be an irreversible inactivator of the tryptophan tryptophylquinone (TTQ) enzyme methylamine dehydrogenase [Davidson, V.L. and Jones, L.H. (1992) Biochim. Biophys. Acta 1121, 104-110]. Structure-reactivity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a03888641a4f09207185d7a4d1cc590
https://doi.org/10.1016/0167-4838(95)00114-a
https://doi.org/10.1016/0167-4838(95)00114-a