Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase
Authors
Keywords
-
Journal
SCIENCE
Volume 358, Issue 6361, Pages 373-377
Publisher
American Association for the Advancement of Science (AAAS)
Online
2017-10-20
DOI
10.1126/science.aan4574
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- RadicalS-Adenosylmethionine Enzymes in Human Health and Disease
- (2016) Bradley J. Landgraf et al. Annual Review of Biochemistry
- Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway
- (2016) John E. Cronan MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS
- Crystallographic snapshots of sulfur insertion by lipoyl synthase
- (2016) Martin I. McLaughlin et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients
- (2016) Andrew Melber et al. eLife
- Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery
- (2015) Nunziata Maio et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactions
- (2014) Jenny E. Harmer et al. BIOCHEMICAL JOURNAL
- Evidence for a Catalytically and Kinetically Competent Enzyme–Substrate Cross-Linked Intermediate in Catalysis by Lipoyl Synthase
- (2014) Nicholas D. Lanz et al. BIOCHEMISTRY
- Physical and Functional Interactions of a Monothiol Glutaredoxin and an Iron Sulfur Cluster Carrier Protein with the Sulfur-donating RadicalS-Adenosyl-l-methionine Enzyme MiaB
- (2013) Sylvain Boutigny et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mutations in Iron-Sulfur Cluster Scaffold Genes NFU1 and BOLA3 Cause a Fatal Deficiency of Multiple Respiratory Chain and 2-Oxoacid Dehydrogenase Enzymes
- (2011) Jessie M. Cameron et al. AMERICAN JOURNAL OF HUMAN GENETICS
- A Fatal Mitochondrial Disease Is Associated with Defective NFU1 Function in the Maturation of a Subset of Mitochondrial Fe-S Proteins
- (2011) Aleix Navarro-Sastre et al. AMERICAN JOURNAL OF HUMAN GENETICS
- Biotin Synthase Exhibits Burst Kinetics and Multiple Turnovers in the Absence of Inhibition by Products and Product-Related Biomolecules
- (2010) Christine E. Farrar et al. BIOCHEMISTRY
- Lipoic Acid Metabolism in Microbial Pathogens
- (2010) M. D. Spalding et al. MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS
- A Complex between Biotin Synthase and the Iron−Sulfur Cluster Assembly Chaperone HscA That Enhances in Vivo Cluster Assembly
- (2009) Michael R. Reyda et al. BIOCHEMISTRY
- Anaerobic functionalization of unactivated C–H bonds
- (2009) Squire J Booker CURRENT OPINION IN CHEMICAL BIOLOGY
- Lipoic Acid Synthesis and Attachment in Yeast Mitochondria
- (2009) Melissa S. Schonauer et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Iron–sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
- (2008) Marc Fontecave et al. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- NfuA, a New Factor Required for Maturing Fe/S Proteins inEscherichia coliunder Oxidative Stress and Iron Starvation Conditions
- (2008) Sandra Angelini et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Biogenesis of Iron-Sulfur Clusters in Photosystem I
- (2008) Zhao Jin et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Proposed Role for theAzotobacter vinelandiiNfuA Protein as an Intermediate Iron-Sulfur Cluster Carrier
- (2008) Sibali Bandyopadhyay et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Fe-S Cluster Assembly Pathways in Bacteria
- (2008) C. Ayala-Castro et al. MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started