David Leitner

Last updated

David M. Leitner is an American chemist currently Professor at University of Nevada, Reno [1] and an Elected Fellow of the American Association for the Advancement of Science. [2]

Contents

Education

He earned his B.S. at Cornell University in 1985 and then his Ph.D at University of Chicago in 1989 under R. Stephen Berry. [3]

Research

His interests are energy-molecule relations and his highest paper is An extended dynamical hydration shell around proteins, [4] according to Google Scholar. [5]

Publications

Related Research Articles

<span class="mw-page-title-main">Cytochrome</span> Redox-active proteins containing a heme with a Fe atom as a cofactor

Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d.

<span class="mw-page-title-main">Solvation</span> Association of molecules of a solvent with molecules or ions of a solute

Solvation describes the interaction of a solvent with dissolved molecules. Both ionized and uncharged molecules interact strongly with a solvent, and the strength and nature of this interaction influence many properties of the solute, including solubility, reactivity, and color, as well as influencing the properties of the solvent such as its viscosity and density. If the attractive forces between the solvent and solute particles are greater than the attractive forces holding the solute particles together, the solvent particles pull the solute particles apart and surround them. The surrounded solute particles then move away from the solid solute and out into the solution. Ions are surrounded by a concentric shell of solvent. Solvation is the process of reorganizing solvent and solute molecules into solvation complexes and involves bond formation, hydrogen bonding, and van der Waals forces. Solvation of a solute by water is called hydration.

<span class="mw-page-title-main">Cytochrome c</span> Protein-coding gene in the species Homo sapiens

The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion. It belongs to the cytochrome c family of proteins and plays a major role in cell apoptosis. Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the respiratory electron transport chain, where it carries one electron. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It transfers electrons between Complexes III and IV. In humans, cytochrome c is encoded by the CYCS gene.

<span class="mw-page-title-main">Molecular engineering</span> Field of study in molecular properties

Molecular engineering is an emerging field of study concerned with the design and testing of molecular properties, behavior and interactions in order to assemble better materials, systems, and processes for specific functions. This approach, in which observable properties of a macroscopic system are influenced by direct alteration of a molecular structure, falls into the broader category of “bottom-up” design.

Bioinorganic chemistry is a field that examines the role of metals in biology. Bioinorganic chemistry includes the study of both natural phenomena such as the behavior of metalloproteins as well as artificially introduced metals, including those that are non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins.

<span class="mw-page-title-main">Heme A</span> Chemical compound

Heme A is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of heme B, a component of hemoglobin, the red pigment in blood.

<span class="mw-page-title-main">Arieh Warshel</span> Israeli chemist, biochemist and biophysicist (born 1940)

Arieh Warshel is an Israeli-American biochemist and biophysicist. He is a pioneer in computational studies on functional properties of biological molecules, Distinguished Professor of Chemistry and Biochemistry, and holds the Dana and David Dornsife Chair in Chemistry at the University of Southern California. He received the 2013 Nobel Prize in Chemistry, together with Michael Levitt and Martin Karplus for "the development of multiscale models for complex chemical systems".

Quantum biology is the study of applications of quantum mechanics and theoretical chemistry to aspects of biology that cannot be accurately described by the classical laws of physics. An understanding of fundamental quantum interactions is important because they determine the properties of the next level of organization in biological systems.

<span class="mw-page-title-main">Cytochrome c oxidase subunit III</span> Enzyme of the respiratory chain encoded by the mitochondrial genome

Cytochrome c oxidase subunit III (COX3) is an enzyme that in humans is encoded by the MT-CO3 gene. It is one of main transmembrane subunits of cytochrome c oxidase. It is also one of the three mitochondrial DNA (mtDNA) encoded subunits of respiratory complex IV. Variants of it have been associated with isolated myopathy, severe encephalomyopathy, Leber hereditary optic neuropathy, mitochondrial complex IV deficiency, and recurrent myoglobinuria.

<span class="mw-page-title-main">CYC1</span> Protein-coding gene in the species Homo sapiens

Cytochrome c1, heme protein, mitochondrial (CYC1), also known as UQCR4, MC3DN6, Complex III subunit 4, Cytochrome b-c1 complex subunit 4, or Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit is a protein that in humans is encoded by the CYC1 gene. CYC1 is a respiratory subunit of Ubiquinol Cytochrome c Reductase, which is located in the inner mitochondrial membrane and is part of the electron transport chain. Mutations in this gene may cause mitochondrial complex III deficiency, nuclear, type 6.

<span class="mw-page-title-main">David E. Clemmer</span>

David E. Clemmer is an analytical chemist and the Distinguished Professor and Robert and Marjorie Mann Chair of Chemistry at Indiana University in Bloomington, Indiana, where he leads the Clemmer Group. Clemmer develops new scientific instruments for ion mobility mass spectrometry (IMS/MS), including the first instrument for nested ion-mobility time-of-flight mass spectrometry. He has received a number of awards, including the Biemann Medal in 2006 "for his pioneering contributions to the integration of ion mobility separations with a variety of mass spectrometry technologies."

Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins. When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside lipid bilayer.

<span class="mw-page-title-main">Martin Gruebele</span>

Martin Gruebele is a German-born American physical chemist and biophysicist who is currently James R. Eiszner Professor of Chemistry, Professor of Physics, Professor of Biophysics and Computational Biology at the University of Illinois at Urbana-Champaign where he is the principal investigator of the Gruebele Group.

<span class="mw-page-title-main">Supercomplex</span>

Modern biological research has revealed strong evidence that the enzymes of the mitochondrial respiratory chain assemble into larger, supramolecular structures called supercomplexes, instead of the traditional fluid model of discrete enzymes dispersed in the inner mitochondrial membrane. These supercomplexes are functionally active and necessary for forming stable respiratory complexes.

<span class="mw-page-title-main">Geraldine L. Richmond</span> American chemist and physicist

Geraldine Lee Richmond is an American chemist and physical chemist who is serving as the Under Secretary of Energy for Science in the US Department of Energy. Richmond was confirmed to her DOE role by the United States Senate on November 5, 2021. Richmond is the Presidential Chair in Science and Professor of Chemistry at the University of Oregon (UO). She conducts fundamental research to understand the chemistry and physics of complex surfaces and interfaces. These understandings are most relevant to energy production, atmospheric chemistry and remediation of the environment. Throughout her career she has worked to increase the number and success of women scientists in the U.S. and in many developing countries in Africa, Asia and South America. Richmond has served as president of the American Association for the Advancement of Science, and she received the 2013 National Medal of Science.

Edmond Chow is an associate professor in the School of Computational Science and Engineering of Georgia Institute of Technology. His main areas of research are in designing numerical methods for high-performance computing and applying these methods to solve large-scale scientific computing problems.

Martina Havenith-Newen is a German chemist.

<span class="mw-page-title-main">Sylvie Roke</span> Dutch chemist and physicist specialized in photochemistry

Sylvie Roke is a Dutch chemist and physicist specialized in photonics and aqueous systems. As a full professor she holds Julia Jacobi Chair of Photomedicine at EPFL and is the director of the Laboratory for fundamental BioPhotonics.

John Russell “Camille” Falck is an American chemist, Professor of Biochemistry, and holder of the Robert A. Welch Distinguish Chair in Chemistry at the University of Texas Southwestern Medical Center. In 1996 he was awarded the Wilfred T. Doherty Recognition Award from the Dallas-Forth Worth Section of the American Chemical Society and a Recognition Award at the March 10, 2002, Winter Eicosanoid Conference in appreciation of his significant contributions to the chemistry of natural products, and to the identification and functional characterization of the cytochrome P450 (P450) arachidonic acid (AA) monooxygenase metabolic pathway and its metabolites.

<span class="mw-page-title-main">Bettie Sue Masters</span> American biochemist

Bettie Sue Siler Masters is an adjunct professor at Duke University known for her work on nitric oxide synthase and cytochrome P450 reductase. She was the 1992 recipient of the FASEB Excellence in Science Award, and has been elected as a member of the National Academy of Medicine and as a fellow of the American Association for the Advancement of Science.

References

  1. "CV" (PDF). unr.edu. Retrieved December 21, 2017.
  2. "Two faculty members named AAAS Fellows". unr.edu. November 21, 2017. Retrieved December 21, 2017.
  3. "David M. Leitner". unr.edu. Retrieved December 21, 2017.
  4. Simon Ebbinghaus, Seung Joong Kim, Matthias Heyden, Xin Yu, Udo Heugen, Martin Gruebele, David M Leitner, Martina Havenith. An extended dynamical hydration shell around proteins. 104:52. 20749-20752. Proceedings of the National Academy of Sciences. 2007
  5. "David Leitner" . Retrieved December 21, 2017.