Zobrazeno 1 - 10
of 148
pro vyhledávání: '"Paul A. Ludden"'
Autor:
Shuyang Zhen, Bruce Bugbee, Lance C. Seefeldt, Paul W. Ludden, Mathangi Soundararajan, Rhesa N. Ledbetter, Scott A. Ensign, Paul Kusuma
Publikováno v:
Frontiers in Microbiology
Frontiers in Microbiology, Vol 10 (2019)
Plants, Soils, and Climate Faculty Publications
Frontiers in Microbiology, Vol 10 (2019)
Plants, Soils, and Climate Faculty Publications
A promising approach for the synthesis of high value reduced compounds is to couple bacteria to the cathode of an electrochemical cell, with delivery of electrons from the electrode driving reductive biosynthesis in the bacteria. Such systems have be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98229ebf52dde706739218e2310974c5
https://doi.org/10.3389/fmicb.2019.01817
https://doi.org/10.3389/fmicb.2019.01817
Autor:
Andrew P Foote, Larry A. Kuehn, Harvey C. Freetly, John W. Kern, John W. Keele, Amanda K. Lindholm-Perry, Paul A. Ludden, Jeremy R. Miles, R. J. Kern, Warren M Snelling, William T. Oliver
Publikováno v:
Gene. 586(1)
Background Feed intake and gain are economically important traits in beef production. The rumen wall interacts with feed, microbial populations, and fermentation products important to cattle nutrition. As such, it is likely to be a critical component
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ca6a2fcd5b3a31543fa1715639fc32e
https://pubmed.ncbi.nlm.nih.gov/27033587
https://pubmed.ncbi.nlm.nih.gov/27033587
Autor:
Paul W. Ludden, Luis M. Rubio
Publikováno v:
Biological Nitrogen Fixation
The iron-molybdenum cofactor (FeMo-co), located at the active site of the molybdenum nitrogenase, is one of the most complex metal cofactors known to date. During the past several years, an intensive effort has been made to purify the proteins involv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59c6e8e1445b29cc28796a9aaed3d8cb
https://doi.org/10.1146/annurev.micro.62.081307.162737
https://doi.org/10.1146/annurev.micro.62.081307.162737
Autor:
Yuming Xiao, Paul W. Ludden, Stephen P. Cramer, Marie Demuez, Simon J. George, Yoshitaka Yoda, Robert Y. Igarashi, Jose A. Hernandez, Luis M. Rubio, Dehua Zhao
Publikováno v:
Journal of the American Chemical Society. 130:5673-5680
NifB-co, an Fe-S cluster produced by the enzyme NifB, is an intermediate on the biosynthetic pathway to the iron molybdenum cofactor (FeMo-co) of nitrogenase. We have used Fe K-edge extended X-ray absorption fine structure (EXAFS) spectroscopy togeth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48df6ab9bb78d3bc9ac762cc51f2b4cc
https://doi.org/10.1021/ja0755358
https://doi.org/10.1021/ja0755358
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1757(12):1582-1591
Upon exposure to CO during anaerobic growth, the purple phototrophic bacterium Rhodospirillum rubrum expresses a CO-oxidizing H 2 evolving enzymatic system. The CO-oxidizing enzyme, carbon monoxide dehydrogenase (CODH), has been purified and extensiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7088f9a338b435cec593f6ddd4125220
Publikováno v:
FEMS Microbiology Letters. 152:195-204
The regulation of nitrogen fixation in Azospirillum brasilense is very complicated, and it responds to exogenous fixed nitrogen or a change of oxygen concentration. This regulation occurs at both transcriptional and posttranslational levels. Unlike r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30b5db819863c425a10b191542e0302f
https://doi.org/10.1111/j.1574-6968.1997.tb10428.x
https://doi.org/10.1111/j.1574-6968.1997.tb10428.x
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 10:903-912
Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum catalyzes the oxidation of CO to CO2. A unique [NiFe4S4] cluster, known as the C-cluster, constitutes the active site of the enzyme. When grown in Ni-deficient medium R. rubrum accumulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d499cb5e5610aa86946396fc8473e1cb
https://doi.org/10.1007/s00775-005-0043-z
https://doi.org/10.1007/s00775-005-0043-z
Autor:
Luis M. Rubio, Paul W. Ludden
Publikováno v:
Journal of Bacteriology. 187:405-414
The nitrogenase enzyme catalyzes the reductive breakage of the very strong triple bond of N2 to generate NH3 in a process known as biological nitrogen fixation. Biological nitrogen fixation is an essential step in the nitrogen cycle in the biosphere,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5643493ede6bcb8e60d197eb12662c8b
https://doi.org/10.1128/jb.187.2.405-414.2005
https://doi.org/10.1128/jb.187.2.405-414.2005
Publikováno v:
Journal of Biological Chemistry. 279:19739-19746
The formation of an active dinitrogenase requires the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized apodinitrogenase. In Azotobacter vinelandii, NafY (also known as gamma protein) has been proposed to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b12a8ebd233f1520302e79550f86bd00
https://doi.org/10.1074/jbc.m400965200
https://doi.org/10.1074/jbc.m400965200
Publikováno v:
Journal of Bacteriology. 184:5894-5897
Substitution of one amino acid for another at the active site of an enzyme usually diminishes or eliminates the activity of the enzyme. In some cases, however, the specificity of the enzyme is changed. In this study, we report that the changing of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10be84e2c3ad311c66a16049605db410
https://doi.org/10.1128/jb.184.21.5894-5897.2002
https://doi.org/10.1128/jb.184.21.5894-5897.2002