Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase

A Abhishek Sirohiwal (Department of Inorganic and Physical Chemistry) J Juliane John (Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences) Y Yury Kutin (Department of Chemistry and Chemical Biology, Technical University Dortmund, Faculty for Chemistry and Chemical Biology) R Rohit Kumar F Federico Baserga (Experimental Molecular Biophysics, Department of Physics, Freie Universität Berlin) V Vivek Srinivas (Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences) H Hugo Lebrette (Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative, CNRS, Université de Toulouse) M Maximilian C. Pöverlein (Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences) A Ana P. Gamiz-Hernandez (Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences) J Joachim Heberle (Experimental Molecular Biophysics, Department of Physics, Freie Universität Berlin) M Müge Kasanmascheff (Department of Chemistry and Chemical Biology, Technical University Dortmund, Faculty for Chemistry and Chemical Biology) M Martin Högbom (Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences) V Ville R. I. Kaila (Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, Stockholm 10691, Sweden)

Abstract

Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotide (RNA) to deoxyribonucleotide (DNA) building blocks initiated by a long-range (>30 Å) proton-coupled electron transfer (PCET) by mechanistic principles that remain much debated. By combining multiscale quantum and classical simulations with directed mutagenesis, X-ray crystallography, and vibrational and electron paramagnetic resonance spectroscopy, we elucidate here the molecular principles underlying how metal-free RNRs initiate the long-range PCET process by creating a highly stable 3,4-dihydroxyphenylalanine (DOPA) initiator radical. We show that DOPA• is redox-tuned by a low-barrier hydrogen bond (LBHB), with a delocalized proton that provides the catalytic power for the ribonucleotide reduction. We find that the LBHB couples to an extended hydrogen-bonded network, with distant mutations resulting in the loss of radical formation, and providing key molecular insight into the long-range radical transport mechanism in RNRs. On a general level, our findings support the direct involvement of LBHB in protein chemistry and the importance of quantum effects in enzyme catalysis.

Article Details

Volume / Issue Vol. 123, Issue 19
Published May 12, 2026
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (13)

A

Abhishek Sirohiwal

Department of Inorganic and Physical Chemistry

J

Juliane John

Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences

Y

Yury Kutin

Department of Chemistry and Chemical Biology, Technical University Dortmund, Faculty for Chemistry and Chemical Biology

R

Rohit Kumar

F

Federico Baserga

Experimental Molecular Biophysics, Department of Physics, Freie Universität Berlin

V

Vivek Srinivas

Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences

H

Hugo Lebrette

Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative, CNRS, Université de Toulouse

M

Maximilian C. Pöverlein

Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences

A

Ana P. Gamiz-Hernandez

Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences

J

Joachim Heberle

Experimental Molecular Biophysics, Department of Physics, Freie Universität Berlin

M

Müge Kasanmascheff

Department of Chemistry and Chemical Biology, Technical University Dortmund, Faculty for Chemistry and Chemical Biology

M

Martin Högbom

Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences

V

Ville R. I. Kaila

Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, Stockholm 10691, Sweden