The Tightly Bound Calcium of MauG Is Required for Tryptophan Tryptophylquinone Cofactor Biosynthesis

Author:

Shin Sooim1,Feng Manliang1,Chen Yan2,Jensen Lyndal M. R.3,Tachikawa Hiroyasu4,Wilmot Carrie M.3,Liu Aimin2,Davidson Victor L.1

Affiliation:

1. Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, United States

2. Department of Chemistry, Georgia State University, Atlanta, Georgia 30302, United States

3. Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 321 Church Street SE, Minneapolis, Minnesota 55455, United States

4. Department of Chemistry, Jackson State University, Jackson, Mississippi 39217, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Cited by 13 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state;Nature Communications;2019-03-07

2. Thermodynamic analysis of MauG, a diheme oxygenase;Applied Biological Chemistry;2017-12-14

3. Equilibrium study of copper absorption to different types of soft contact lens;Applied Biological Chemistry;2017-04

4. A simple method to engineer a protein-derived redox cofactor for catalysis;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2014-10

5. Bis-Fe(IV): nature’s sniper for long-range oxidation;JBIC Journal of Biological Inorganic Chemistry;2014-04-11

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