A Sulfur Oxygenase from the Haloalkaliphilic Bacterium Thioalkalivibrio Paradoxus with Atypically Low Reductase Activity

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2016 Dec 7

PMID 27920296

Citations 6

Authors

Patrick Ruhl

Uwe Poll

Johannes Braun

Andreas Klingl

Arnulf Kletzin

Affiliations

Soon will be listed here.

Abstract

Importance: Sulfur oxygenase reductases (SORs) are the only enzymes catalyzing an oxygen-dependent disproportionation of elemental sulfur and/or polysulfides to sulfite, thiosulfate, and hydrogen sulfide. SORs are known from mesophilic and extremophilic archaea and bacteria. All SORs seem to form highly thermostable 24-subunit hollow spheres. They carry a low-potential mononuclear nonheme iron in the active site and an indispensable cysteine; however, their exact reaction mechanisms are unknown. Typically, the reductase activity of SORs is in the range of 5 to 50% of the oxygenase activity, but mutagenesis studies had so far failed to identify residues crucial for the reductase reaction. We describe here the first SOR, which is almost devoid of the reductase reaction and which comes from a haloalkaliphilic bacterium.

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