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Paul W. Ludden
Researcher at University of California, Berkeley
Publications - 152
Citations - 7744
Paul W. Ludden is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Rhodospirillum rubrum & Azotobacter vinelandii. The author has an hindex of 51, co-authored 152 publications receiving 7456 citations. Previous affiliations of Paul W. Ludden include University of Wisconsin-Madison & Midwestern University.
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Biosynthesis of the iron-molybdenum cofactor of nitrogenase.
Luis M. Rubio,Paul W. Ludden +1 more
TL;DR: In this paper, an intensive effort has been made to purify the proteins involved in FeMo-co synthesis and incorporation into nitrogenase, and this effort is starting to provide insights into the structures of the FeMoco biosynthetic intermediates and into the biochemical details of FeMoCo synthesis.
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Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.
TL;DR: This x-ray structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems.
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Carbon monoxide-dependent growth of Rhodospirillum rubrum.
TL;DR: Under dark, anaerobic conditions in the presence of sufficient nickel, Rhodospirillum rubrum grows with a doubling time of under 5 h by coupling the oxidation of CO to the reduction of H+ to H2.
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Maturation of Nitrogenase: a Biochemical Puzzle
Luis M. Rubio,Paul W. Ludden +1 more
TL;DR: 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, and it is a major contributor to the nitrogen cycle.
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Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum.
TL;DR: In the photosynthetic bacterium Rhodospirillum rubrum, the presence of carbon monoxide (CO) induces expression of several proteins, such as CODH and CO-tolerant hydrogenase as mentioned in this paper.