Metal Coordination Dynamics Governs Selective Halogenation in α‐KG/Fe‐Dependent Halogenase SyrB2

W Wenli Yuan (Beijing National Laboratory for Molecular Sciences, CAS Laboratory of Colloid and Interface and Thermodynamics, CAS Research/Education Center for Excellence in Molecular Sciences, Center for Carbon Neutral Chemistry) J Jiayong Huang J Jia Liu J Jianqiang Feng (Institute of Molecular Engineering Plus, College of Chemistry, Fuzhou University 2 , Fuzhou 350108,) S Shengheng Yan (State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering) L Lina Dong (State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China) Y Yangyang Song (Qingdao Institute for Theoretical and Computational Sciences and Center for Optics Research and Engineering Shandong University Qingdao P. R. China) Z Zikuan Wang (Max-Planck-Institut für Kohlenforschung) X Xiaoyun Xiao L Lanteng Wang (State Key Laboratory of Quantitative Synthetic Biology) J Jiahai Zhou (School of Food Science and Pharmaceutical Engineering) S Sason Shaik (Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, Jerusalem 9190401, Israel) B Binju Wang (State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering)

Abstract

ABSTRACT α‐Ketoglutarate (α‐KG)‐dependent nonheme iron enzymes catalyze a diverse array of oxidative transformations essential for natural product biosynthesis. However, the mechanism by which α‐KG/Fe‐dependent halogenases achieve selective halogenation while circumventing the thermodynamically favored hydroxylation pathway remains a subject of intense debate. In this study, we elucidate the halogenation mechanism in SyrB2 through extensive computational and crystallographic investigations. Our work reveals that metal coordination dynamics plays a pivotal role in controlling selective C─H bond activation and chlorination in SyrB2. The transformation of the Fe(IV)‐oxo species from an equatorial to an axial conformation enables hydrogen atom transfer from the substrate C─H bond. Subsequent re‐isomerization of the Fe(III)‐OH intermediate to the equatorial conformation is critical for promoting selective chlorination while minimizing competitive hydroxylation. The proposed mechanism is supported by multiple experimental observations, including Mössbauer spectroscopy, nuclear resonance vibrational spectroscopy (NRVS), 2 H‐HYSCORE spectroscopy, and kinetic analysis of reactions with various substrates.

Article Details

Volume / Issue Vol. 1, Issue 1
Published August 12, 2026
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (13)

W

Wenli Yuan

Beijing National Laboratory for Molecular Sciences, CAS Laboratory of Colloid and Interface and Thermodynamics, CAS Research/Education Center for Excellence in Molecular Sciences, Center for Carbon Neutral Chemistry

J

Jiayong Huang

J

Jia Liu

J

Jianqiang Feng

Institute of Molecular Engineering Plus, College of Chemistry, Fuzhou University 2 , Fuzhou 350108,

S

Shengheng Yan

State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering

L

Lina Dong

State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China

Y

Yangyang Song

Qingdao Institute for Theoretical and Computational Sciences and Center for Optics Research and Engineering Shandong University Qingdao P. R. China

Z

Zikuan Wang

Max-Planck-Institut für Kohlenforschung

X

Xiaoyun Xiao

L

Lanteng Wang

State Key Laboratory of Quantitative Synthetic Biology

J

Jiahai Zhou

School of Food Science and Pharmaceutical Engineering

S

Sason Shaik

Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, Jerusalem 9190401, Israel

B

Binju Wang

State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering