Persulfide Dioxygenase From Acidithiobacillus caldus: Variable Roles of Cysteine Residues and Hydrogen Bond Networks of the Active Site

Persulfide Dioxygenase From Acidithiobacillus caldus: Variable Roles of Cysteine Residues and Hydrogen Bond Networks of the Active Site

Persulfide dioxygenases (PDOs) are abundant in Bacteria and also crucial for H2S detoxification in mitochondria. One of the two pdo-genes of the acidophilic bacterium Acidithiobacillus caldus was expressed in Escherichia coli. The protein (AcPDO) had 0.77 ± 0.1 Fe/subunit and an average specific sul...

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Bibliographic Details
Main Authors: Patrick Rühl, Patrick Haas, Dominik Seipel, Jan Becker, Arnulf Kletzin
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-07-01
Series:Frontiers in Microbiology
Subjects:
persulfide dioxygenase
sulfhydryl
sulfur
enzyme kinetics
differential scanning fluorimetry
ETHE1
Online Access:https://www.frontiersin.org/article/10.3389/fmicb.2018.01610/full

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https://www.frontiersin.org/article/10.3389/fmicb.2018.01610/full

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