A Second Soluble Hox-Type NiFe Enzyme Completes the Hydrogenase Set in Thiocapsa roseopersicina BBS-Reference-Cited by-同舟云学术

A Second Soluble Hox-Type NiFe Enzyme Completes the Hydrogenase Set in Thiocapsa roseopersicina BBS

Published:2010-08 Issue:15 Volume:76 Page:5113-5123
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Maróti Judit¹,Farkas Attila²,Nagy Ildikó K.²,Maróti Gergely²,Kondorosi Éva²,Rákhely Gábor¹³,Kovács Kornél L.¹³

Affiliation:

1. Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Szeged 6726, Hungary

2. BayGen Institute, Bay Zoltán Foundation for Applied Research, Derkovits fasor 2, Szeged 6726, Hungary

3. Department of Biotechnology, University of Szeged, Közép fasor 52, Szeged 6726, Hungary

Abstract

ABSTRACT Three functional NiFe hydrogenases were previously characterized in Thiocapsa roseopersicina BBS: two of them are attached to the periplasmic membrane (HynSL and HupSL), and one is localized in the cytoplasm (HoxEFUYH). The ongoing genome sequencing project revealed the presence of genes coding for another soluble Hox-type hydrogenase enzyme ( hox2FUYH ). Hox2 is a heterotetrameric enzyme; no indication for an additional subunit was found. Detailed comparative in vivo and in vitro activity and expression analyses of HoxEFUYH (Hox1) and the newly discovered Hox2 enzyme were performed. Functional differences between the two soluble NiFe hydrogenases were disclosed. Hox1 seems to be connected to both sulfur metabolism and dark/photofermentative processes. The bidirectional Hox2 hydrogenase was shown to be metabolically active under specific conditions: it can evolve hydrogen in the presence of glucose at low sodium thiosulfate concentration. However, under nitrogen-fixing conditions, it can oxidize H 2 but less than the other hydrogenases in the cell.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/AEM.00351-10

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