Structure and Kinetic Analysis of H₂S Production by Human Mercaptopyruvate Sulfurtransferase

Authors

Pramod Kumar Yadav, Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan
Kazuhiro Yamada, Uniformed Services University of the Health Sciences
Taurai Chiku, Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan
Markos Koutmos, Uniformed Services University of the Health Sciences
Ruma V. Banerjee, University of Michigan Medical CenterFollow

Date of this Version

2013

Citation

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 288, NO. 27, pp. 20002–20013, July 5, 2013

Comments

US government work

Abstract

Background: Mercaptopyruvate sulfurtransferase (MST) generates H₂S, a signaling molecule.

Results: The detailed kinetics and crystal structure of human MST with bound substrate are reported.

Conclusion: Thioredoxin is the preferred persulfide acceptor from MST.

Significance: The structure provides molecular insights into activation and stabilization of MST reaction intermediates.