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

Journal Article · · Science
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [2];  [3]; ORCiD logo [4]
  1. Univ. of Illinois at Urbana-Champaign, IL (United States). Center for Biophysics and Quantitative Biology
  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)

Metals brought together do more Enzymatic reduction of oxyanions such as sulfite (SO 3 2− ) requires the delivery of multiple electrons and protons, a feat accomplished by cofactors tailored for catalysis and electron transport. Replicating this strategy in protein scaffolds may expand the range of enzymes that can be designed de novo. Mirts et al. selected a scaffold protein containing a natural heme cofactor and then engineered a cavity suitable for binding a second cofactor—an iron-sulfur cluster (see the Perspective by Lancaster). The resulting designed enzyme was optimized through rational mutation into a catalyst with spectral characteristics and activity similar to that of natural sulfite reductases. Science , this issue p. 1098 ; see also p. 1071

Research Organization:
Univ. of Illinois at Urbana-Champaign, IL (United States); Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Center for Advanced Bioenergy and Bioproducts Innovation (CABBI), Urbana, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS)
Contributing Organization:
SLAC National Accelerator Laboratory (SLAC); Karolinska Institute
Grant/Contract Number:
SC0018420; R01-GM062211; 5T32-GM827625; AC02-76SF00515
OSTI ID:
1470758
Alternate ID(s):
OSTI ID: 1991812
Journal Information:
Science, Vol. 361, Issue 6407; ISSN 0036-8075
Publisher:
AAASCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 84 works
Citation information provided by
Web of Science

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Cited By (10)

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
Unraveling the enzyme-like activity of heterogeneous single atom catalyst journal January 2019
Reactivity of Small Oxoacids of Sulfur 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
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
Why does sulfite reductase employ siroheme? journal January 2019
Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters journal July 2019
The importance of catalytic promiscuity for enzyme design and evolution journal November 2019
Artificial Metalloenzymes: Challenges and Opportunities journal July 2019
Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin journal January 2019

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