ReviewBiochimica et biophysica acta2016
Structural principles for computational and de novo design of 4Fe-4S metalloproteins.
Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022Article
- Changing the tracks: screening for electron transfer proteins to support hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR.Frontiers in molecular biosciences · 2022Article
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I.iScience · 2021Article
- Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites.Angewandte Chemie (International ed. in English) · 2020Article
- Radical S-adenosylmethionine maquette chemistry: CxJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters.Molecules (Basel, Switzerland) · 2019Review
- Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer.Journal of the American Chemical Society · 2018Article
- Green Rust: The Simple Organizing 'Seed' of All Life?Life (Basel, Switzerland) · 2018Review
- Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster.Biopolymers · 2018Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Iron-sulfur centers in metalloproteins can access multiple oxidation states over a broad range of potentials, allowing them to participate in a variety of electron transfer reactions and serving as catalysts for high-energy redox processes. The nitrogenase FeMoCO cluster converts di-nitrogen to ammonia in an eight-electron transfer step. The 2(Fe4S4) containing bacterial ferredoxin is an evolutionarily ancient metalloprotein fold and is thought to be a primordial progenitor of extant oxidoreductases. Controlling chemical transformations mediated by iron-sulfur centers such as nitrogen fixation, hydrogen production as well as electron transfer reactions involved in photosynthesis are of tremendous importance for sustainable chemistry and energy production initiatives. As such, there is significant interest in the design of iron-sulfur proteins as minimal models to gain fundamental understanding of complex natural systems and as lead-molecules for industrial and energy applications. Herein, we discuss salient structural characteristics of natural iron-sulfur proteins and how they guide principles for design. Model structures of past designs are analyzed in the context of these principles and potential directions for enhanced designs are presented, and new areas of iron-sulfur protein design are proposed. This article is part of a Special issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, protein networks, edited by Ronald L. Koder and J.L Ross Anderson.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.