Basic Information

 

 

黄钢锋  教授         

生命科学与技术学院  

西安交通大学青年拔尖人才(A类)

         

Prof. Dr. Gangfeng Huang

School of Life Science and Technology

Xi'an Jiaotong University

 

Contact Information

地址:西安交通大学创新港18-4034

 

邮编:712046

 

邮件:gangfeng.haung@xjtu.edu.cn

 

 

Institute of Analytical Chemistry and Instrument for Life Science, The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology,Xi'an Jiaotong University, Xi'an 712046, China.

Email: gangfeng.huang@xjtu.edu.cn

 

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Research Fields

Education

Postdoc. & Ph.D. in Microbial protein structure group lead by Dr. Seigo Shima of Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.

Research interests

During my academic position, I worked on anaerobic microbes in agriculture and key enzymes in the metabolism of complex organic matter of agriculture. During education, my main research goal is to analyze the properties and catalytic mechanism of [Fe]-hydrogenase using X-ray crystallographic, biochemical, and spectroscopic methods. In addition, I worked on the analysis of semi-synthetic [Fe]-hydrogenase using chemical mimic compounds of [Fe]-hydrogenase cofactor and building of artificial hydrogenases in hydrogenation catalysis.

 

  1. Catalytic mechanism of [Fe]-hydrogenase from methanogenic archaea.

   

  1. Huang G#, Wagner T#, Wodrich MD, Ataka K, Bill E, Ermler U, et al. The atomic-resolution crystal structure of activated [Fe]-hydrogenase. Nature Catalysis 2019, 2(6): 537-543. (Cover story
  2. Huang G, Wagner T, Ermler U, Shima S. Methanogenesis involves direct hydride transfer from H2 to an organic substrate. Nature Reviews Chemistry 2020, 4(4): 213-221. (Cover story)

  1. Construction of semi-synthetic [Fe]-/[Mn]-hydrogenase.

    

  1. Pan HJ, Huang G, Wodrich MD, Tirani FF, Ataka K, Shima S, et al. A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor. Nature Chemistry 2019, 11(7): 669-675.
  2. Huang G, Arriaza-Gallardo FJ, Wagner T, Shima S. Crystal structures of [Fe]-hydrogenase from Methanolacinia paynteri suggest a path of the FeGP-cofactor incorporation process. Inorganics 2020, 8(9): 50. (Cover story)
  3. Pan HJ, Huang G, Wodrich MD, Tirani FF, Ataka K, Shima S, et al. Diversifying metal-ligand cooperative catalysis in semi-synthetic [Mn]-hydrogenases. Angewandte Chemie International Edition 2021, 133(24): 13462-13469.
  4. Wang C, Lai Z, Huang G*, Pan HJ*. Current State of [Fe]-hydrogenase and its biomimetic models. Chemistry – A European Journal 2022, 28(57): e202285761. 

  1. O2 sensitivity of [Fe]-hydrogenase and its protection.

  1. Huang G, Wagner T, Ermler U, Bill E, Ataka K, Shima S. Dioxygen sensitivity of [Fe]-hydrogenase in the presence of reducing substrates. Angewandte Chemie International Edition 2018, 57(18): 4917-4920.
  2. Wagner T#, Huang G#, Ermler U, Shima S. How [Fe]-hydrogenase from Methanothermobacter is protected against light and oxidative stress. Angewandte Chemie International Edition 2018, 57(46): 15056-15059.

 

Main methods

 

Biochemical analysis (enzyme kinetics), gene mutation analysis (site-directed mutagenesis), protein structure analysis (X-ray crystallography), spectroscopy (infrared spectroscopy, electron paramagnetic resonance, Mössbauer spectroscopy); computational chemistry (DFT, QM/MM), etc.