WorldCat Identities

Andrade, Susana L. A.

Works: 9 works in 13 publications in 1 language and 1,130 library holdings
Roles: dgs, Contributor, Other
Classifications: QP535.F4, 570
Publication Timeline
Most widely held works by Susana L. A Andrade
Iron-sulfur clusters in chemistry and biology by Tracey A Rouault( )

5 editions published in 2014 in English and held by 1,072 WorldCat member libraries worldwide

This volume on iron-sulfur clusters includes chapters that cover the history of the discovery of iron-sulfur clusters in the 1960s to discoveries of their role in the enzyme, aconitase (1980s), and numerous other proteins. It explains basic chemistry principles, how microbes, plants, and animals synthesize these complex prosthetic groups, and why it is important to understand the chemistry and biogenesis of FeS proteins
Structural characterization of the two copper proteins nitrous oxide reductase from Pseudomonas stutzeri and laccase Lcc5 from Coprinopsis cinerea by Anja Pomowski( )

1 edition published in 2011 in English and held by 13 WorldCat member libraries worldwide

Although, the reduction of nitrous oxide (N2O) is highly exergonic, a high activation barrier hinders a spontaneous reaction. With regard to inertness, N2O is second only to molecular nitrogen and in both cases a complex metal center is required for activation. The only known enzyme, which catalyzes the reduction of N2O to N2 is the oxygen sensitive copper-protein nitrous oxide reductase (N2OR). Crystallographic studies on this enzyme from Paracoccus denitrificans, Marinobacter hydrocarbonoclasticus and Achromobacter cycloclastes provided insight into its structure: The protein forms a head-to-tail homodimer, which was shown to be obligatory for enzyme reaction. Each monomer comprises of two distinct domains, an N-terminal ß-propeller with the tetranuclear CuZ site and a C-terminal cupredoxin-like domain carrying the mixed valent CuA center, similar to the one found in cytochrome c oxidase. However, these structures represent the aerobically isolated protein, which is only active upon extended incubation with reducing agents. In contrast, the purple form of nitrous oxide reductase from Pseudomonas stutzeri shows physiological activity without the necessity of reductive activation. This work presents the first structure of the purple form of nitrous oxide reductase and as well the first structure of a metal-N2O complex, providing new insights into the binding mode of N2O to the catalytic site. In pressurized crystals N2O binds between CuZ and CuA site, which is as previously described a mixed-valent center alternating between the oxidized mixed-valent [Cu+1.5:Cu+1.5] and the reduced [Cu+:Cu+] state thereby providing one electron per cycle. In contrast to previous structures, the histidine ligand of CuA1 is flexible and rotates to form hydrogen bonds with a near-by serine and aspartate residue in dependence of substrate binding
Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement by Thomas Spatzal( )

1 edition published in 2016 in English and held by 3 WorldCat member libraries worldwide

Abstract: The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catalyses the 6-electron reduction of dinitrogen to ammonium in biological nitrogen fixation. Only recently its atomic structure was clarified, while its reactivity and electronic structure remain under debate. Here we show that for its resting S=3/2 state the common iron oxidation state assignments must be reconsidered. By a spatially resolved refinement of the anomalous scattering contributions of the 7 Fe atoms of FeMoco, we conclude that three irons (Fe1/3/7) are more reduced than the other four (Fe2/4/5/6). Our data are in agreement with the recently revised oxidation state assignment for the molybdenum ion, providing the first spatially resolved picture of the resting-state electron distribution within FeMoco. This might provide the long-sought experimental basis for a generally accepted theoretical description of the cluster that is in line with available spectroscopic and functional data
Electrophysiological characterization of Ammonium transport proteins by Tobias Wacker( )

1 edition published in 2015 in English and held by 2 WorldCat member libraries worldwide

Zusammenfassung: Die Stickstoffaufnahme in reduzierter Form, als Ammonium ist innerhalb einer kompetitiven Umwelt ein essenzieller biologischer Prozess vorkommend in Prokaryonten, Archaeen und Pflanzen. Der NH₄⁺ /NH₃-Transport über biologische Membranen wird mittels einer ubiquitären, integralen Membranproteinfamilie gewährleistet, den sogenannten Ammoniumtransportproteinen (Amt-Proteine). Bisher wurden mehrere Kristallstrukturen in Kombination mit funktionellen Daten von Mitgliedern dieser Proteinfamilie erhalten. Die funktionellen Daten wurden mittels Zweielektroden basierten Patch-Clamp Messungen an Xenopus Oozyten, in vivo radioaktiv Messungen und in vivo pH-Messungen in Proteoliposomen erhalten. Dennoch war es bisher nicht möglich das transportierte Substrat, sowie mechanistische Details des Transportprozesses zu ermitteln. Im Rahmen dieser Arbeit wurde ein reproduzierbarer, verlässlicher und kontrollierter in vitro Messaufbau für die drei homologen Amt Proteine des hyperthermophilen Organismus Archaeoglobus fulgidus etabliert. In Folge dessen wurden die drei rekombinant überproduzierten Amt Proteine Af-Amt1-3 aufgereinigt und in bereits vorgeformte Liposomen rekonstituiert. Die Proteoliposomen wurden mittels Gefrierbruch-Transmissionselektronenmikroskopie analysiert und mittels zweier unterschiedlicher elektrophysiologischer Techniken untersucht. Geringe Transportraten verhinderten jedoch eine funktionelle elektrophysiologische Charakterisierung mittels freistehender planarer Lipiddoppelmembran (sog. Planar Lipid Bilayer, PLB), wohingegen Messungen mittels einer festphasenunterstützten Membran (sog. Solid Supported Membrane, SSM) in überzeugender Weise, die ersten verlässlichen in vitro Ergebnisse liefern konnte. Diese Arbeit bestätigte unmissverständlich einen elektrogenen Substrattransport für Af-Amt1 und Af-Amt3 und beschreibt die vollständige Charakterisierung beider Proteine in einem pH-equilibrierten System bei Nullspannung. Die SSM-Messungen verdeutlichen die funktionellen Unterschiede beider Proteine in Bezug auf die pH-Abhängigkeit, relative Transportraten und die Substrataffinitäten
Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion by Daniel Sippel( )

1 edition published in 2016 in English and held by 2 WorldCat member libraries worldwide

Structural rearrangements during copper cluster insertion into nitrous oxide reductase of Pseudomonas stutzeri by Anja Wüst( )

1 edition published in 2016 in English and held by 2 WorldCat member libraries worldwide

Signaling ammonium across membranes through an ammonium sensor histidine kinase by Tobias Pflüger( )

1 edition published in 2017 in English and held by 2 WorldCat member libraries worldwide

Audience Level
Audience Level
  Kids General Special  
Audience level: 0.16 (from 0.12 for Iron-sulfu ... to 0.97 for Iron-sulfu ...)

Iron-sulfur clusters in chemistry and biology
Alternative Names
Andrade, Susana L.A. 1972-

Susana L A Andrade wetenschapper

English (13)