ReviewBiochimica et biophysica acta2016
Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.
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 72 papers.
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Who cites it
72 citing papers in PubMed, 192 citations in OpenAlex.
- A Divergent Mitochondrial Cytochrome c in Malaria Parasites With an Anomalously Low Redox Potential.Journal of molecular biology · 2026Article
- Azurins With Tunable Reduction Potentials as Redox Mediators for Extracellular Electron Transfer.Chembiochem : a European journal of chemical biology · 2026Article
- From the Cosmos to the Cell: The Central Role of Iron in the Chemistry and Evolution of Life.International journal of molecular sciences · 2026Review
- Directed evolution of APOX for proximity labeling using phenols with high redox potentials.Cell chemical biology · 2026Article
- Exploring the Influence of Electronic Structure on Electrocatalytic Nitrate Reduction to Ammonia.Chemistry, an Asian journal · 2026Review
- A Divergent CytochromebioRxiv : the preprint server for biology · 2025Article
- Role of Propionate Side Chain in Heme-Containing Metalloenzymes.ACS organic & inorganic Au · 2025Review
- Predicting Metalloprotein Redox Potentials with Machine Learning: A Focus on Iron-Sulfur Systems.Journal of chemical information and modeling · 2025Article
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- Two Key Ferredoxins for Nitrogen Fixation Have Different Specificities and Biophysical Properties.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Deciphering reductive dehalogenase specificity through targeted mutagenesis of chloroalkane reductases.Applied and environmental microbiology · 2025Article
- Electrocatalytic Nitrite Reduction by a Monomeric NrfA: Commonality in Ammonification Mechanisms.Biochemistry · 2025Article
- Structure Bioinformatics of Six Human Integral Transmembrane Enzymes and their AlphaFold3 Predicted Water-Soluble QTY Analogs: Insights into FACE1 and STEA4 Binding Mechanisms.Pharmaceutical research · 2025Article
- De Novo design of α-helical heme binding proteins capable of versatile cofactor ligation.Methods in enzymology · 2025Article
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.Protein science : a publication of the Protein Society · 2024Article
- The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Complex I activity in hypoxia: implications for oncometabolism.Biochemical Society transactions · 2024Review
- The structure of the diheme cytochrome cJournal of inorganic biochemistry · 2024Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Redox potentials are a major contributor in controlling the electron transfer (ET) rates and thus regulating the ET processes in the bioenergetics. To maximize the efficiency of the ET process, one needs to master the art of tuning the redox potential, especially in metalloproteins, as they represent major classes of ET proteins. In this review, we first describe the importance of tuning the redox potential of ET centers and its role in regulating the ET in bioenergetic processes including photosynthesis and respiration. The main focus of this review is to summarize recent work in designing the ET centers, namely cupredoxins, cytochromes, and iron-sulfur proteins, and examples in design of protein networks involved these ET centers. We then discuss the factors that affect redox potentials of these ET centers including metal ion, the ligands to metal center and interactions beyond the primary ligand, especially non-covalent secondary coordination sphere interactions. We provide examples of strategies to fine-tune the redox potential using both natural and unnatural amino acids and native and nonnative cofactors. Several case studies are used to illustrate recent successes in this area. Outlooks for future endeavors are also provided. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.
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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.