SULFUR OXIDATION AND REDUCTION IN ARCHAEA - SULFUR OXYGENASE REDUCTASE AND HYDROGENASES FROM THE EXTREMELY THERMOPHILIC AND FACULTATIVELY ANAEROBIC ARCHAEON DESULFUROLOBUS-AMBIVALENS/
A. Kletzin, SULFUR OXIDATION AND REDUCTION IN ARCHAEA - SULFUR OXYGENASE REDUCTASE AND HYDROGENASES FROM THE EXTREMELY THERMOPHILIC AND FACULTATIVELY ANAEROBIC ARCHAEON DESULFUROLOBUS-AMBIVALENS/, Systematic and applied microbiology, 16(4), 1994, pp. 534-543
The sulfur-dependent, chemolithotrophic, extremely thermophilic, acido
philic, and facultatively anaerobic Archaeon Desulfurolobus ambivalens
was examined for enzymes involved in energy metabolism. A soluble sul
fur oxygenase/-reductase (SOR) was purified and characterized. This en
zyme was not detectable in anaerobically grown cells. It produced simu
ltaneously sulfite and HIS from sulfur in the presence of oxygen and i
s part of the sulfur-oxidizing pathway of the organism. The gene encod
ing the single subunit was cloned, sequenced and transcriptionally ana
lyzed. Hydrogenase activities were found in cytoplasmic and membrane f
ractions of aerobically and of anaerobically grown cells. In non-denat
uring gels six different protein bands with hydrogenase activity were
detected. The membrane-bound hydrogenase of anaerobically grown cells
was investigated in detail, and the presence and distribution of sulfu
r reductases, rhodaneses and cytochromes were analyzed. The results of
this study are compared to other sulfur-metabolizing enzymes from Arc
haea and models of sulfur oxidation and reduction pathways are discuss
ed.