ArticleJournal of the American Chemical Society2014
Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 93 citations in OpenAlex.
- Expression and Engineering of Conductive Cytochrome Nanowires.bioRxiv : the preprint server for biology · 2026Article
- Direct electrochemistry as a mechanistic tool for studying engineered myoglobins: implications on carbene transferase activity.Dalton transactions (Cambridge, England : 2003) · 2026Article
- Toward Understanding Ligand-Directed Excited-State Electron Flow in Bridged Ruthenium(II) Complexes.Inorganic chemistry · 2025Article
- Role of Propionate Side Chain in Heme-Containing Metalloenzymes.ACS organic & inorganic Au · 2025Review
- Unveiling an Ultrareduced State of Heme in Myoglobin.Journal of the American Chemical Society · 2025Article
- Engineering Gel-Based Precursors into Advanced ORR Catalysts for Zn-Air Batteries and Fuel Cells: Insights into Hydrogels, Aerogels, Xerogels, Metal-Organic Gels, and Metal Aerogels.Gels (Basel, Switzerland) · 2025Review
- Controlling heme redox properties in peptide amphiphile fibers with sequence and heme loading ratio.Biophysical journal · 2024Article
- Fluctuation Relations to Calculate Protein Redox Potentials from Molecular Dynamics Simulations.Journal of chemical theory and computation · 2024Article
- Electrochemical and structural characterization of recombinant respiratory proteins of the acidophilic iron oxidizerFrontiers in microbiology · 2024Article
- Mechanistic and structural characterization of an iridium-containing cytochrome reveals kinetically relevant cofactor dynamics.Nature catalysis · 2023Article
- Integrating UV-Vis Spectroscopy and Oxygen Optode for Accurate Determination of Oxygen Affinity of Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Enantioselective Synthesis of α-Trifluoromethyl Amines via Biocatalytic N-H Bond Insertion with Acceptor-Acceptor Carbene Donors.Journal of the American Chemical Society · 2022Article
- Chemical modifications of proteins and their applications in metalloenzyme studies.Synthetic and systems biotechnology · 2021Review
- An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network.Biochemistry · 2021Article
- Strategies for the expression and characterization of artificial myoglobin-based carbene transferases.Methods in enzymology · 2020Article
- Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping.Journal of the American Chemical Society · 2019Article
- Stereoselective Cyclopropanation of Electron-Deficient Olefins with a Cofactor Redesigned Carbene Transferase Featuring Radical Reactivity.ACS catalysis · 2019Article
- Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors.Accounts of chemical research · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Cytochrome c Oxidase (CcO) is known to catalyze the reduction of O2 to H2O efficiently with a much lower overpotential than most other O2 reduction catalysts. However, methods by which the enzyme fine-tunes the reduction potential (E°) of its active site and the corresponding influence on the O2 reduction activity are not well understood. In this work, we report systematic tuning of the heme E° in a functional model of CcO in myoglobin containing three histidines and one tyrosine in the distal pocket of heme. By removing hydrogen-bonding interactions between Ser92 and the proximal His ligand and a heme propionate, and increasing hydrophobicity of the heme pocket through Ser92Ala mutation, we have increased the heme E° from 95 ± 2 to 123 ± 3 mV. Additionally, replacing the native heme b in the CcO mimic with heme a analogs, diacetyl, monoformyl, and diformyl hemes, that posses electron-withdrawing groups, resulted in higher E° values of 175 ± 5, 210 ± 6, and 320 ± 10 mV, respectively. Furthermore, O2 consumption studies on these CcO mimics revealed a strong enhancement in O2 reduction rates with increasing heme E°. Such methods of tuning the heme E° through a combination of secondary sphere mutations and heme substitutions can be applied to tune E° of other heme proteins, allowing for comprehensive investigations of the relationship between E° and enzymatic activity.
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