Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Matthew J. Ryle"'
Autor:
Robert P. Hausinger, Lawrence Que, Kevin D. Koehntop, Aimin Liu, Rajendra Bose Muthukumaran, Matthew J. Ryle, Raymond Y. N. Ho, John McCracken
Publikováno v:
Biochemistry. 42:1854-1862
Taurine/alpha-ketoglutarate dioxygenase (TauD), a non-heme mononuclear Fe(II) oxygenase, liberates sulfite from taurine in a reaction that requires the oxidative decarboxylation of alpha-ketoglutarate (alphaKG). The lilac-colored alphaKG-Fe(II)TauD c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5327a9fe25bc8bff770041e6091357b8
https://doi.org/10.1021/bi026832m
https://doi.org/10.1021/bi026832m
Autor:
Jack E. Baldwin, Matthew J. Ryle, Julie C. Dunning Hotopp, Robert P. Hausinger, Nicolai I. Burzlaff, Peter L. Roach, Ian J. Clifton, Jonathan M. Elkins, John S. Lloyd
Publikováno v:
Biochemistry. 41:5185-5192
Taurine/alpha-ketoglutarate dioxygenase (TauD), a non-heme Fe(II) oxygenase, catalyses the conversion of taurine (2-aminoethanesulfonate) to sulfite and aminoacetaldehyde concurrent with the conversion of alpha-ketoglutarate (alphaKG) to succinate an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c1845a5d9267392a06331653a1a301d
https://doi.org/10.1021/bi016014e
https://doi.org/10.1021/bi016014e
Autor:
Lawrence Que, Eric L. Hegg, Mark P. Mehn, Aimin Liu, Matthew J. Ryle, Raymond Y. N. Ho, Robert P. Hausinger
Publikováno v:
Journal of the American Chemical Society. 123:5022-5029
The bidentate coordination of an alpha-keto acid to an iron(II) center via the keto group and the carboxylate gives rise to metal-to-ligand charge-transfer transitions between 400 and 600 nm in model complexes and in alpha-ketoglutarate-dependent dio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30fe11c612e0541b35f128e41182322d
https://doi.org/10.1021/ja0041775
https://doi.org/10.1021/ja0041775
Autor:
James B. Howard, Douglas C. Rees, Hsiu-Ju Chiu, William N. Lanzilotta, John W. Peters, Lance C. Seefeldt, Matthew J. Ryle
Publikováno v:
Biochemistry. 40:641-650
A mutant form of the nitrogenase iron protein with a deletion of residue Leu 127, located in the switch II region of the nucleotide binding site, forms a tight, inactive complex with the nitrogenase molybdenum iron (MoFe) protein in the absence of nu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3f9440ec84459909bbdedee9e164a43
https://doi.org/10.1021/bi001645e
https://doi.org/10.1021/bi001645e
Publikováno v:
Journal of Bacteriology. 182:2597-2603
In a number of nitrogen-fixing bacteria, nitrogenase is posttranslationally regulated by reversible ADP-ribosylation of dinitrogenase reductase. The structure of the dinitrogenase reductase from Azotobacter vinelandii is known. In this study, mutant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1cea9b08b94b60a24ba6e5d71f03033
https://doi.org/10.1128/jb.182.9.2597-2603.2000
https://doi.org/10.1128/jb.182.9.2597-2603.2000
Publikováno v:
Biochemistry. 38:15278-15286
Taurine/alpha-ketoglutarate dioxygenase (TauD), a member of the broad class of non-heme Fe(II) oxygenases, converts taurine (2-aminoethanesulfonate) to sulfite and aminoacetaldehyde while decomposing alpha-ketoglutarate (alphaKG) to form succinate an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9c654bd9d0ba4994bb9cfd4c01152b2
https://doi.org/10.1021/bi9912746
https://doi.org/10.1021/bi9912746
Autor:
William N. Lanzilotta, Dennis R. Dean, Paul W. Ludden, Paul J. Goodwin, Priya Rangaraj, Matthew J. Ryle, Vinod K. Shah
Publikováno v:
Journal of Biological Chemistry. 274:29413-29419
Besides serving as the obligate electron donor to dinitrogenase during nitrogenase turnover, dinitrogenase reductase (NifH) is required for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) and for the maturation of alpha(2)beta(2) apo-dinit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23a7c62e772d5123ede33f993735ba85
https://doi.org/10.1074/jbc.274.41.29413
https://doi.org/10.1074/jbc.274.41.29413
In Vitro Biosynthesis of Iron-Molybdenum Cofactor and Maturation of the nif-encoded Apodinitrogenase
Publikováno v:
Journal of Biological Chemistry. 274:19778-19784
NifH has three different roles in the nitrogenase enzyme system. Apart from serving as the physiological electron donor to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in maturation of the FeMo-co-deficient f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b8d61a63b88252bf22bf268eae25088
https://doi.org/10.1074/jbc.274.28.19778
https://doi.org/10.1074/jbc.274.28.19778
Autor:
William N. Lanzilotta, Matthew J. Ryle, Robert C. Scarrow, Gerard M. Jensen, Lance C. Seefeldt
Publikováno v:
Journal of Biological Chemistry. 271:1551-1557
Nucleotide interactions with nitrogenase are a central part of the mechanism of nitrogen reduction. Previous studies have suggested that MgATP or MgADP binding to the nitrogenase iron protein (Fe protein) induce protein conformational changes that co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e6a337f80f310a44f7b241bd391ff55
https://doi.org/10.1074/jbc.271.3.1551
https://doi.org/10.1074/jbc.271.3.1551
Publikováno v:
Biochemistry. 35:9424-9434
Nucleotide binding to the nitrogenase iron (Fe) protein results in a lowering of the redox potential of its [4Fe-4S] cluster by over 100 mV, and this is thought to be essential for electron transfer to the molybdenum-iron (MoFe) protein for substrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b70d6d87441e606f6a3f4857a42e8a4d
https://doi.org/10.1021/bi9608572
https://doi.org/10.1021/bi9608572