Author
Severo Ochoa
Other affiliations: University of Minnesota, United States Public Health Service, Spanish National Research Council ...read more
Bio: Severo Ochoa is an academic researcher from Roche Institute of Molecular Biology. The author has contributed to research in topics: Initiation factor & RNA. The author has an hindex of 73, co-authored 239 publications receiving 15574 citations. Previous affiliations of Severo Ochoa include University of Minnesota & United States Public Health Service.
Papers published on a yearly basis
Papers
More filters
547 citations
TL;DR: The discovery of carbon dioxide assimilation by heterotrophic bacteria and animal tissues aroused considerable interest in the mechanisms involved and Evans, Vennesland, and Slotin discovered that pigeon liver extracts fixed in the presence of malate, pyruvate, and catalytic amounts of manganous ions and of either diphosphopyridine nucleotide (DPN) or triphosphoyridineucleotide (TPN), while catalyzing the overall Reaction 1.
469 citations
TL;DR: The metabolic utilization of acetate (oxidation via the citric acid cycle, synthesis of higher fatty acids, cholesterol, and possibly other compounds) requires a preliminary activation through conversion to acetyl C0A, and two main mechanisms are known to bring about this activation.
402 citations
TL;DR: This report from the Department of Biochemistry at the New York University School of Medicine examines the agreement found between experimentally determined letters of the genetic code and amino acid replacement methods in nitrous acid mutants of the tobacco mosaic virus.
Abstract: This report from the Department of Biochemistry at the New York University School of Medicine examines the agreement found
between experimentally determined letters of the genetic code and amino acid replacement methods in nitrous acid mutants of
the tobacco mosaic virus (TMV).
385 citations
Cited by
More filters
01 Jan 1969
10,262 citations
TL;DR: The application of numerical methods are presented to enable the trivially parallel solution of the Poisson-Boltzmann equation for supramolecular structures that are orders of magnitude larger in size.
Abstract: Evaluation of the electrostatic properties of biomolecules has become a standard practice in molecular biophysics. Foremost among the models used to elucidate the electrostatic potential is the Poisson-Boltzmann equation; however, existing methods for solving this equation have limited the scope of accurate electrostatic calculations to relatively small biomolecular systems. Here we present the application of numerical methods to enable the trivially parallel solution of the Poisson-Boltzmann equation for supramolecular structures that are orders of magnitude larger in size. As a demonstration of this methodology, electrostatic potentials have been calculated for large microtubule and ribosome structures. The results point to the likely role of electrostatics in a variety of activities of these structures.
6,918 citations
TL;DR: Dehydroisomerization of Limonene and Terpenes To Produce Cymene 2481 4.2.1.
Abstract: 3.2.3. Hydroformylation 2467 3.2.4. Dimerization 2468 3.2.5. Oxidative Cleavage and Ozonolysis 2469 3.2.6. Metathesis 2470 4. Terpenes 2472 4.1. Pinene 2472 4.1.1. Isomerization: R-Pinene 2472 4.1.2. Epoxidation of R-Pinene 2475 4.1.3. Isomerization of R-Pinene Oxide 2477 4.1.4. Hydration of R-Pinene: R-Terpineol 2478 4.1.5. Dehydroisomerization 2479 4.2. Limonene 2480 4.2.1. Isomerization 2480 4.2.2. Epoxidation: Limonene Oxide 2480 4.2.3. Isomerization of Limonene Oxide 2481 4.2.4. Dehydroisomerization of Limonene and Terpenes To Produce Cymene 2481
5,127 citations
TL;DR: The results are shown to favour the ferryl ion structure, or an isomer of this structure, for the higher oxidation state, and theHigher oxidation state may provisionally be named ferrylmyoglobin.
Abstract: more acidic solutions, with pH < 7 0, a few seconds elapsed before equilibrium was attained. Taking into account the ionization of the haem-linked group on MetMb and the higher oxidation state, the variation of Kb,. with pH is shown to confirm the conclusion that 2 moles ofH+ are liberated/mole of acidic MetMb. Using 6-1 for the pK of the group in MetMb as established in other studies, the results give apK of75 for the group in the higher oxidation state at 200 and I= 0 04. 3. The variation of KRb, with temperature gives AHO = 10-0 ± 2*0 kcal./g.mol.: if the ionization of the haem-linked group is allowed for, the value 9*0 ± 1.0 kcal./g.mol. is obtained. 4. The dependence of Kob. on ionic strength is in accord with a change in charge from + 1 on MetMb to zero on the higher oxidation state. 5. The results are shown to favour the ferryl ion structure, or an isomer of this structure, for the higher oxidation state. The isomeric structures would, in general, require the presence of another ionizing group in myoglobin, but no evidence for such an ionization could be found. With other direct evidence favouring the ferryl ion structure this is to be preferred, and the higher oxidation state may provisionally be named ferrylmyoglobin.
3,654 citations