Zobrazeno 1 - 10
of 112
pro vyhledávání: '"L E Mortenson"'
Publikováno v:
Current Microbiology. 30:351-355
The putative products of six Azotobacter vinelandii chromosomal open reading frames (ORFs) were suggested to be involved in dihydrogen (H2) metabolism [Chen and Mortenson (1992) Biochim Biophys Acta 1131, 199-202]. A promoterless lacZ-containing cass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fa4f8112301107f9119419ccf7bc47f
https://doi.org/10.1007/bf00369862
https://doi.org/10.1007/bf00369862
Publikováno v:
Journal of Biological Chemistry. 270:13112-13117
Biological nitrogen fixation catalyzed by purified nitrogenase requires the hydrolysis of a minimum of 16 MgATP for each N2 reduced. In the present study, we demonstrate a central function for Lys-15 of Azotobacter vinelandii nitrogenase iron protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::880f2bba9a72ac7db87d92de431c4301
https://doi.org/10.1074/jbc.270.22.13112
https://doi.org/10.1074/jbc.270.22.13112
Autor:
Drozdzewski Pm, He Sh, L. E. Mortenson, Harry D. Peck, T.V. Morgan, Juszczak A, Jean LeGall, Weiguang Fu, DerVartanian Dv, Michael W. W. Adams
Publikováno v:
Biochemistry. 32:4813-4819
The nature of the iron-sulfur clusters in oxidized and reduced forms of Fe-only hydrogenases from Desulfovibrio vulgaris, Thermotoga maritima, and Clostridium pasteurianum has been investigated by resonance Raman spectroscopy. The results indicate th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06e06dffa3e51c3454d926f5ed1ec33d
https://doi.org/10.1021/bi00069a016
https://doi.org/10.1021/bi00069a016
Publikováno v:
Proceedings of the National Academy of Sciences. 90:1078-1082
Nitrogenase (EC 1.18.6.1) catalyzes the conversion of dinitrogen to ammonia, the central reaction of biological nitrogen fixation. X-ray anomalous diffraction data were analyzed to probe the structures of the metal clusters bound by nitrogenase MoFe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6e2de52c0d57aad24384176fe8c92fc
https://doi.org/10.1073/pnas.90.3.1078
https://doi.org/10.1073/pnas.90.3.1078
Autor:
L. E. Mortenson, Lance C. Seefeldt
Publikováno v:
Protein Science. 2:93-102
MgATP-binding and hydrolysis are an integral part of the nitrogenase catalytic mechanism. We are exploring the function of MgATP hydrolysis in this reaction by analyzing the properties of the Fe protein (FeP) component of Azotobacter vinelandii nitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2bcfbbfbbf7df5078d6c51beecb19b57
https://doi.org/10.1002/pro.5560020110
https://doi.org/10.1002/pro.5560020110
Publikováno v:
Journal of Bacteriology. 174:4549-4557
Azotobacter vinelandii contains a heterodimeric, membrane-bound [NiFe]hydrogenase capable of catalyzing the reversible oxidation of H2. The beta and alpha subunits of the enzyme are encoded by the structural genes hoxK and hoxG, respectively, which a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c7c44d756bfd64f6a26681f3adc5a3e
https://doi.org/10.1128/jb.174.14.4549-4557.1992
https://doi.org/10.1128/jb.174.14.4549-4557.1992
Autor:
Jack Chien Chen, L. E. Mortenson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1131:199-202
We reported earlier the identification of two Azotobacter vinelandii open reading frames (ORFs), ORF1 and ORF2, downstream from the hydrogenase structural genes (Chen, J.C. and Mortenson, L.E. (1992) Biochim. Biophys. Acta 1131, 122–124). Sequencin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e59c79acc67ed14eddf8a2dbfbecd392
https://doi.org/10.1016/0167-4781(92)90077-d
https://doi.org/10.1016/0167-4781(92)90077-d
Publikováno v:
Journal of Biological Chemistry. 267:6680-6688
Nitrogenase binds and hydrolyzes 2MgATP yielding 2MgADP and 2Pi for each electron that is transferred from the iron protein to the MoFe protein. The iron protein alone binds but does not hydrolyze 2MgATP or 2MgADP and the binding of these nucleotides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e3bec783c57b31cbe28102d62cb707e3
https://doi.org/10.1016/s0021-9258(19)50480-x
https://doi.org/10.1016/s0021-9258(19)50480-x
Publikováno v:
Journal of Magnetic Resonance (1969). 91:227-240
The molybdenum-iron (MoFe) protein of nitrogenase from Clostridium pasteurianum forms monoclinic crystals in space group P21. The unit cell comprises two molecules, each of which possesses a molecular twofold symmetry axis and binds two chemically id
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1f6ead8cd6d7f36b6ae2fe1b81f8053
https://doi.org/10.1016/0022-2364(91)90188-y
https://doi.org/10.1016/0022-2364(91)90188-y
Autor:
W. B. Mims, Jack Peisach, L. E. Mortenson, John McCracken, William H. Orme-Johnson, T. V. Morgan
Publikováno v:
Biochemistry. 29:3077-3082
Mg-ATP binds to the iron protein component of nitrogenase. The magnetic field dependence of the linear electric field effect (LEFE) in pulsed EPR is consistent with a single 4Fe-4S cluster. The LEFE is virtually unaltered when Mg-ATP is bound. Electr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4f3a495755569481467b6df4ad8d92f
https://doi.org/10.1021/bi00464a026
https://doi.org/10.1021/bi00464a026