Applied Biological Chemistry

, Volume 61, Issue 1, pp 73–78 | Cite as

Thermodynamic analysis of MauG, a diheme oxygenase

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Abstract

MauG is a unique c-type diheme oxygenase. One heme of MauG is five-coordinate and solvent accessible with His53 as axial ligand, while the other heme of MauG is six-coordinate with His205 and Tyr294. MauG catalyzes posttranslational modification including oxygen insertion, cross-linkage of two tryptophan and oxidation of quinol to quinone of precursor methylamine dehydrogenase (preMADH) to form mature tryptophan tryptophylquinone (TTQ) which is one of protein-derived cofactors. Long-range remote catalysis of substrate is possible without direct contact between hemes of MauG and its substrate, preMADH. Although catalytic properties and mechanisms of MauG have been well studied, temperature dependence of MauG has never been reported yet. Therefore, the objective of this study was to perform thermodynamic analysis of MauG. ΔH° of 87.6 ± 6.7 kJ mol−1 and ΔS° of 232 ± 15.6 J mol−1 K−1 were directly measured for oxidized MauG in this study. Those results provide fundamental information on controlling electron transfer rates for biosynthesis of TTQ in MADH and are used as a good thermodynamic example study for other diheme systems.

Keywords

C-type diheme enzyme MauG Oxygenase Thermodynamic parameters 

Notes

Acknowledgments

This work was supported by NRF Grants (2016R1C1B1008673 and 2016R1C1B2008836).

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Copyright information

© The Korean Society for Applied Biological Chemistry 2017

Authors and Affiliations

  1. 1.Interdisciplinary Program of Bioenergy and Biomaterials Graduate School (BK21 Plus Program), Department of Biotechnology and Bioengineering, College of EngineeringChonnam National UniversityGwangjuRepublic of Korea
  2. 2.Department of Optometry, College of Energy and BiotechnologySeoul National University of Science and TechnologySeoulRepublic of Korea

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