rubredoxin — LLMpedia

rubredoxin
Jawahar Swaminathan and MSD staff at the European Bioinformatics Institute · Public domain · source
Name	Rubredoxin

Contents

rubredoxin

Introduction

Rubredoxin is a small iron–sulfur electron-transfer protein first characterized in studies linking Max Perutz-era structural biology to redox biochemistry and later examined in laboratories associated with Frederick Sanger and Linus Pauling. Early experimental reports emerged alongside work at institutions such as the Medical Research Council and the Max Planck Society, and the protein became a model in structural studies performed at facilities like the European Molecular Biology Laboratory and the Brookhaven National Laboratory. Seminal methods developed at the University of Cambridge and the California Institute of Technology aided its high-resolution analysis, enabling connections to classic biochemical treatments described in texts from the Royal Society and the National Academy of Sciences.

The three-dimensional fold of rubredoxin was resolved using techniques refined at the Royal Institution and the Weizmann Institute of Science, integrating approaches pioneered by groups at the MRC Laboratory of Molecular Biology and the Karolinska Institute. The protein typically adopts a compact topology dominated by a core of beta-strands and loop regions studied with spectroscopy at the Max Planck Institute for Biophysical Chemistry and crystallography at the European Synchrotron Radiation Facility. Central to its chemistry is a single iron center tetrahedrally coordinated by four cysteinyl thiolates; the coordination geometry was elucidated through collaborative efforts including teams from the Lawrence Berkeley National Laboratory and the Argonne National Laboratory. Key publications appearing in journals supported by the American Chemical Society and the Royal Society of Chemistry detailed metal–ligand interactions, corroborated by NMR studies from laboratories at the University of Oxford and the University of California, San Diego.

Rubredoxin functions primarily as an electron carrier in anaerobic and microaerophilic organisms frequently isolated and characterized by investigators associated with the Scripps Research Institute and the Max Planck Institute for Marine Microbiology. It participates in redox reactions connected to pathways investigated by teams at the University of Tokyo and the University of Copenhagen, often interfacing with enzymes studied at the Max Planck Institute for Biochemistry and the Wageningen University. Roles include participation in hydrocarbon degradation processes explored by researchers from the United States Geological Survey and in sulfur metabolism researched at the University of Bergen and the Institut Pasteur. Physiological contexts include function in extremophiles examined by expeditions linked to the Smithsonian Institution and collaborations with the National Oceanic and Atmospheric Administration.

Assembly pathways for the iron center of rubredoxin have been probed using genetic and biochemical tools developed in laboratories at the Massachusetts Institute of Technology and the University of Pennsylvania, and by molecular genetics groups at the University of British Columbia and the Johns Hopkins University. Studies implicating chaperones and sulfur trafficking systems emerged from collaborations involving the Max Planck Institute for Molecular Genetics and the Conseil National de la Recherche Scientifique. Mechanistic models were supported by mutational analyses performed at the Cold Spring Harbor Laboratory and in vitro reconstitution carried out at the Vanderbilt University and the University of Heidelberg.

Comparative genomics surveys performed by consortia including the Human Genome Project-era centers and the Joint Genome Institute mapped rubredoxin-like sequences across bacteria and archaea, with evolutionary analyses undertaken at the European Bioinformatics Institute and the National Center for Biotechnology Information. Phylogenetic patterns indicate divergence events studied in collaboration with researchers at the University of California, Berkeley and the Swiss Federal Institute of Technology Zurich, and lateral gene transfer scenarios were modeled by groups at the Santa Fe Institute and the Max Planck Institute for Evolutionary Anthropology. Structural conservation highlighted in work from the Protein Data Bank and the International Union of Crystallography underscores an ancient origin consistent with metabolic reconstructions published by teams at the Lawrence Livermore National Laboratory.

Rubredoxin and engineered variants have been applied in redox catalysis initiatives supported by enterprise partnerships with the Biotechnology and Biological Sciences Research Council and technology transfer offices at the Massachusetts Institute of Technology. Biotechnological exploitation includes use as a model redox module in synthetic biology projects at the Wyss Institute and the Broad Institute, and incorporation into biosensors developed in collaborative programs with the National Institutes of Health and the Defense Advanced Research Projects Agency. Structural templates have been utilized in directed-evolution campaigns run by labs at the University of Illinois Urbana-Champaign and in biocatalysis scale-up work at the Fraunhofer Society.

Category:Iron–sulfur proteins