Zobrazeno 1 - 10
of 106
pro vyhledávání: '"F. S. Mathews"'
The x-ray structure of the monotopic membrane protein (S)-mandelate dehydrogenase (MDH) from Pseudomonas putida reveals an inherent flexibility of its membrane binding segment that might be important for its biological activity. The surface of MDH ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1ff592eee618de8ea106f38e6faa597
https://europepmc.org/articles/PMC6204087/
https://europepmc.org/articles/PMC6204087/
Publikováno v:
Proceedings of the National Academy of Sciences. 107:6817-6822
The joint x-ray/neutron diffraction model of the Type I copper protein, amicyanin from Paracoccus denitrificans was determined at 1.8 Å resolution. The protein was crystallized using reagents prepared in D 2 O. About 86% of the amide hydrogen atoms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc7084349ed323ab10c85f925e065245
https://doi.org/10.1073/pnas.0912672107
https://doi.org/10.1073/pnas.0912672107
Autor:
F. S. Mathews, Bharati Mitra, Angelo Merli, Gian Luigi Rossi, A. Dewanti, Narayanasami Sukumar
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 65:543-552
(S)-Mandelate dehydrogenase (MDH) from Pseudomonas putida, a membrane-associated flavoenzyme, catalyzes the oxidation of (S)-mandelate to benzoylformate. Previously, the structure of a catalytically similar chimera, MDH-GOX2, rendered soluble by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e29b46998ccdf5eef73b0fec27a233
https://doi.org/10.1107/s0907444909010270
https://doi.org/10.1107/s0907444909010270
Autor:
Narayanasami Sukumar, F. S. Mathews, Kanagalaghatta R. Rajashankar, Steven E. Ealick, David H. Alpers, Marilyn M. Gordon, Zhi-wei Chen
Publikováno v:
Proceedings of the National Academy of Sciences. 104:17311-17316
The structure of intrinsic factor (IF) in complex with cobalamin (Cbl) was determined at 2.6-Å resolution. The overall fold of the molecule is that of an α 6 /α 6 barrel. It is a two-domain protein, and the Cbl is bound at the interface of the do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e7e000ee046334ae8bc4510a36b4745
https://doi.org/10.1073/pnas.0703228104
https://doi.org/10.1073/pnas.0703228104
Autor:
Jonathan P. Hosler, Victor L. Davidson, William E. Antholine, F. S. Mathews, Christopher J. Carrell, J.K. Ma
Publikováno v:
Biochemistry. 46:1900-1912
Amicyanin from Paracoccus denitrificans is a type 1 copper protein with three strong equatorial copper ligands provided by nitrogens of His53 and His95 and the sulfur of Cys92, with an additional weak axial ligand provided by the sulfur of Met98. Met
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68ff7e5a6b00cbe9937fc797bc5487d5
https://doi.org/10.1021/bi0619674
https://doi.org/10.1021/bi0619674
Publikováno v:
Biochemistry. 44:15444-15450
Monomeric sarcosine oxidase (MSOX) is a flavoprotein that contains covalently bound FAD [8a-(S-cysteinyl)FAD] and catalyzes the oxidation of sarcosine (N-methylglycine) and other secondary amino acids, such as l-proline. Our previous studies showed t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::622ba2082d6c5fc809994f27c75246f0
https://doi.org/10.1021/bi0515422
https://doi.org/10.1021/bi0515422
Publikováno v:
Biochemistry. 44:1521-1531
Long chain hydroxy acid oxidase (LCHAO) is a member of an FMN-dependent enzyme family that oxidizes L-2-hydroxy acids to ketoacids. LCHAO is a peroxisomal enzyme, and the identity of its physiological substrate is unclear. Mandelate is the most effic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc10554623bdd4b4188041eedd546995
https://doi.org/10.1021/bi048616e
https://doi.org/10.1021/bi048616e
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 8:843-854
The X-ray structure of methanol dehydrogenase (MEDH) from Paracoccus denitrificans (MEDH-PD) was determined at 2.5 A resolution using molecular replacement based on the structure of MEDH from Methylophilus methylotrophus W3A1 (MEDH-WA). The overall s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f26609414bee0e928492ba0fc9d855c
https://doi.org/10.1007/s00775-003-0485-0
https://doi.org/10.1007/s00775-003-0485-0
Autor:
Zhi-wei Chen, F. S. Mathews, F E Welsh, J.D Barton, Graeme A Reid, Stephen K Chapman, L. M. Cunane
Publikováno v:
Biochemistry. 41:4264-4272
Flavocytochrome b2 catalyzes the oxidation of l-lactate to pyruvate and the transfer of electrons to cytochrome c. The enzyme consists of a flavin-binding domain, which includes the active site for lacate oxidation, and a b2-cytochrome domain, requir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e29f49c2cfa1c7c38f9947a8775b5973
https://doi.org/10.1021/bi0119870
https://doi.org/10.1021/bi0119870
Autor:
Kenji Kano, F. S. Mathews, Mori Y, Shun'ichi Kuroda, Kawaguchi K, Zhi-wei Chen, Tokuji Ikeda, Katsuyuki Tanizawa, Takagi K, Saumen Datta, Toshihide Okajima
Publikováno v:
Proceedings of the National Academy of Sciences. 98:14268-14273
Fluorescence superquenching is investigated for polyelectrolytes consisting of cyanine dye pendant polylysines ranging in number of polymer repeat units (N(PRU)) from 1 to 900, both in solution and after adsorption onto silica nanoparticles. As N(PRU
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55ea820e46f877c6270a6f8738d99587
https://doi.org/10.1073/pnas.241429098
https://doi.org/10.1073/pnas.241429098