WorldCat Identities

Spatzal, Thomas

Works: 5 works in 11 publications in 1 language and 1,096 library holdings
Roles: Author, Contributor, Other
Classifications: QP535.F4, 612.3924
Publication Timeline
Most widely held works by Thomas Spatzal
Iron-sulfur clusters in chemistry and biology by Tracey A Rouault( )

5 editions published in 2014 in English and held by 1,070 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
Identification of a spin-coupled Mo(III) in the nitrogenase iron-molybdenum cofactor by Ragnar Björnsson( )

1 edition published in 2014 in English and held by 3 WorldCat member libraries worldwide

Abstract: Nitrogenase is the enzyme responsible for the catalytic reduction of dinitrogen (N2) to ammonia. In contrast to the industrial Haber-Bosch process that reacts N2 and H2 at high temperature and pressure, the biological reduction proceeds at ambient temperature and pressure using a complex multicomponent protein system, which utilizes eight electrons, eight protons and 16 MgATP molecules.1,2 Unraveling the structural and mechanistic details of how nature activates the strong bond of dinitrogen is of fundamental importance and this knowledge could aid in the design of better catalysts
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
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

Audience Level
Audience Level
  General Special  
Audience level: 0.14 (from 0.12 for Iron-sulfu ... to 0.97 for Iron-sulfu ...)

WorldCat IdentitiesRelated Identities
Iron-sulfur clusters in chemistry and biology
English (11)