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A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme

Journal Article · · Science
 [1];  [2];  [2];  [3];  [4]
  1. Univ. of Illinois at Urbana-Champaign, IL (United States). Center for Biophysics and Quantitative Biology; University of Illinois at Urbana-Champaign
  2. Univ. of Illinois at Urbana-Champaign, IL (United States)
  3. Univ. of Illinois at Urbana-Champaign, IL (United States). School of Chemical Sciences Electron Paramagnetic Resonance Lab.
  4. Univ. of Illinois at Urbana-Champaign, IL (United States). Center for Biophysics and Quantitative Biology, Dept. of Chemistry, Dept. of Biochemistry, Carl R. Woese Inst. for Genomic Biology and Center for Advanced Bioenergy and Bioproducts Innovation (CABBI); Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
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Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement, but it is challenging to design artificial enzymes to catalyze these important reactions, owing to their structural and functional complexity. Here, we report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved—through rational tuning of the secondary sphere interactions around the [4Fe-4S] and the substrate-binding sites—to be close to that of the native enzyme. By offering insight into the requirements for a demanding six-electron, seven-proton reaction that has so far eluded synthetic catalysts, this study provides strategies for designing highly functional multicofactor artificial enzymes.
Research Organization:
Center for Advanced Bioenergy and Bioproducts Innovation (CABBI), Urbana, IL (United States); Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Univ. of Illinois at Urbana-Champaign, IL (United States)
Sponsoring Organization:
National Institute of General Medical Sciences (NIGMS); National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
Contributing Organization:
Karolinska Institute; SLAC National Accelerator Laboratory (SLAC)
Grant/Contract Number:
AC02-76SF00515; SC0018420
OSTI ID:
1470758
Alternate ID(s):
OSTI ID: 1490222
OSTI ID: 1991812
Journal Information:
Science, Journal Name: Science Journal Issue: 6407 Vol. 361; ISSN 0036-8075
Publisher:
AAASCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (10)

Artificial Metalloenzymes: Challenges and Opportunities journal July 2019
Molecular Dynamics Simulation and Kinetic Study of Fluoride Binding to V21C/V66C Myoglobin with a Cytoglobin-like Disulfide Bond journal April 2020
Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters journal July 2019
Reactivity of Small Oxoacids of Sulfur journal July 2019
The importance of catalytic promiscuity for enzyme design and evolution journal November 2019
Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin journal January 2019
Unraveling the enzyme-like activity of heterogeneous single atom catalyst journal January 2019
Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases journal January 2019
Why does sulfite reductase employ siroheme? journal January 2019
Chicken fat for catalysis: a scaffold is as important for molecular complexes for energy transformations as it is for enzymes in catalytic function journal January 2019

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