G. Lewis

Bio: G. Lewis is an academic researcher from University of Southampton. The author has contributed to research in topics: Surface roughness & Dry etching. The author has an hindex of 5, co-authored 10 publications receiving 206 citations.

X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase

Abstract: 5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme that catalyses the formation of porphobilinogen from 5-aminolaevulinic acid. The structure of the yeast enzyme has been solved to 2.3 A resolution, revealing that each subunit adopts a TIM barrel fold with a 39 residue N-terminal arm. Pairs of monomers wrap their arms around each other to form compact dimers and these associate to form a 422 symmetric octamer. All eight active sites are on the surface of the octamer and possess two lysine residues (210 and 263), one of which, Lys 263, forms a Schiff base link to the substrate. The two lysine side chains are close to two zinc binding sites one of which is formed by three cysteine residues (133, 135 and 143) while the other involves Cys 234 and His 142. ALAD has features at its active site that are common to both metallo- and Schiff base-aldolases and therefore represents an intriguing combination of both classes of enzyme. Lead ions, which inhibit ALAD potently, replace the zinc bound to the enzyme's unique triple-cysteine site.

Atom chip for BEC interferometry

Abstract: We have fabricated and tested an atom chip that operates as a matter wave interferometer. In this communication we describe the fabrication of the chip by ion-beam milling of gold evaporated onto a silicon substrate. We present data on the quality of the wires, on the current density that can be reached in the wires and on the smoothness of the magnetic traps that are formed. We demonstrate the operation of the interferometer, showing that we can coherently split and recombine a Bose–Einstein condensate with good phase stability.

Fabrication of Magnetooptical Atom Traps on a Chip

Abstract: Ultracold atoms can be manipulated using microfabricated devices known as atom chips. These have significant potential for applications in sensing, metrology, and quantum information processing. To date, the chips are loaded by transfer of atoms from an external macroscopic magnetooptical trap (MOT) into microscopic traps on the chip. This transfer involves a series of steps, which complicate the experimental procedure and lead to atom losses. In this paper, we present a design for integrating a MOT into a silicon wafer by combining a concave pyramidal mirror with a square wire loop. We describe how an array of such traps has been fabricated, and we present magnetic, thermal, and optical properties of the chip.

Fabrication of Magneto-Optical Atom Traps on a Chip

Abstract: Ultra-cold atoms can be manipulated using microfabricated devices known as atom chips. These have significant potential for applications in sensing, metrology and quantum information processing. To date, the chips are loaded by transfer of atoms from an external, macroscopic magneto-optical trap (MOT) into microscopic traps on the chip. This transfer involves a series of steps, which complicate the experimental procedure and lead to atom losses. In this paper we present a design for integrating a MOT into a silicon wafer by combining a concave pyramidal mirror with a square wire loop. We describe how an array of such traps has been fabricated and we present magnetic, thermal and optical properties of the chip.

ICP polishing of silicon for high-quality optical resonators on a chip

Abstract: Miniature concave hollows, made by wet etching silicon through a circular mask, can be used as mirror substrates for building optical micro-cavities on a chip. In this paper, we investigate how inductively coupled plasma (ICP) polishing improves both shape and roughness of the mirror substrates. We characterize the evolution of the surfaces during the ICP polishing using white-light optical profilometry and atomic force microscopy. A surface roughness of 1 nm is reached, which reduces to 0.5 nm after coating with a high reflectivity dielectric. With such smooth mirrors, the optical cavity finesse is now limited by the shape of the underlying mirror.

Antimicrobial activity of metals: mechanisms, molecular targets and applications

Abstract: Metals have been used as antimicrobial agents since antiquity, but throughout most of history their modes of action have remained unclear. Recent studies indicate that different metals cause discrete and distinct types of injuries to microbial cells as a result of oxidative stress, protein dysfunction or membrane damage. Here, we describe the chemical and toxicological principles that underlie the antimicrobial activity of metals and discuss the preferences of metal atoms for specific microbial targets. Interdisciplinary research is advancing not only our understanding of metal toxicity but also the design of metal-based compounds for use as antimicrobial agents and alternatives to antibiotics.

Zinc coordination sphere in biochemical zinc sites

Abstract: Zinc is known to be indispensable to growth and development and transmission of the genetic message. It does this through a remarkable mosaic of zinc binding motifs that orchestrate all aspects of metabolism. There are now nearly 200 three dimensional structures for zinc proteins, representing all six classes of enzymes and covering a wide range of phyla and species. These structures provide standards of reference for the identity and nature of zinc ligands in other proteins for which only the primary structure is known. Three primary types of zinc sites are apparent from examination of these structures: structural, catalytic and cocatalytic. The most common amino acids that supply ligands to these sites are His, Glu, Asp and Cys. In catalytic sites zinc generally forms complexes with water and any three nitrogen, oxygen and sulfur donors with His being the predominant amino acid chosen. Water is always a ligand to such sites. Structural zinc sites have four protein ligands and no bound water molecule. Cys is the preferred ligand in such sites. Cocatalytic sites contain two or three metals in close proximity with two of the metals bridged by a side chain moiety of a single amino acid residue, such as Asp, Glu or His and sometimes a water molecule. Asp and His are the preferred amino acids for these sites. No Cys ligands are found in such sites. The scaffolding of the zinc sites is also important to the function and reactivity of the bound metal. The influence of zinc on quaternary protein structure has led to the identification of a fourth type of zinc binding site, protein interface. In this case zinc sites are formed from ligands supplied from amino acid residues residing in the binding surface of two proteins. The resulting zinc site usually has the coordination properties of a catalytic or structural zinc binding site.

Enzymes of chlorophyll biosynthesis

Abstract: The enzymes responsible for chlorophyll biosynthesis in plants, algae and cyanobacteria are identified and described, with emphasis on their protein composition and structure, required cofactors, physical and catalytic properties, protein-protein interactions and allosteric modulation of activity. Properties and features of the pathway that enable it to operate in a coordinated way while using unstable and light-sensitive intermediates in potentially hostile biochemical environments are discussed. The evolutionary relationships and possible origins of the chlorophyll biosynthetic enzymes are also discussed.

Protein design: toward functional metalloenzymes.

Abstract: 1. Overview A 2. Protein Redesign B 2.1. Making Use of Native Proteins: Protein Redesign B 2.2. Protein Redesign Based on Functions C 2.2.1. Redesign of Zinc Finger Structural Sites C 2.2.2. Redesign of Zinc Hydrolytic Centers E 2.2.3. Redesign of Heme Centers J 2.2.4. Redesign of Nonheme Redox Centers M 2.2.5. Artificial Metalloenzymes for Regioand Enantioselective Catalysis AA 2.2.6. Redesigned Protein Assemblies as Nanoreactors AK 2.3. Summary AN 3. De Novo Design AN 3.1. A Minimalist Approach: Designing Proteins from Scratch AN 3.2. Interactions between De Novo Designed Peptides and Metal Ions AN 3.2.1. Heavy Metal Toxicity AO 3.2.2. De Novo Designed Metal Centers Based on β-Structures AT 3.2.3. Metal-Induced Protein Folding AV 3.3. De Novo Designed Functional Metalloproteins: The Grail Quest of Protein Design AX 3.3.1. De Novo Designed Hydrolytic Centers AX 3.3.2. De Novo Designed Electron Transfer Centers BB 3.3.3. Other Catalytic Centers BG 3.4. Summary BN 4. Perspective BO Author Information BO Corresponding Author BO Notes BO Biographies BO Abbreviations BR References BR