Characterization of a Heme-Dependent Catalase from Methanobrevibacter arboriphilus†

AUTOR(ES)

Shima, Seigo

FONTE

American Society for Microbiology

RESUMO

Recently it was reported that methanogens of the genus Methanobrevibacter exhibit catalase activity. This was surprising, since Methanobrevibacter species belong to the order Methanobacteriales, which are known not to contain cytochromes and to lack the ability to synthesize heme. We report here that Methanobrevibacter arboriphilus strains AZ and DH1 contained catalase activity only when the growth medium was supplemented with hemin. The heme catalase was purified and characterized, and the encoding gene was cloned. The amino acid sequence of the catalase from the methanogens is most similar to that of Methanosarcina barkeri.

Documentos Relacionados

• Enterococcus faecalis Heme-Dependent Catalase
• Chloroquine inhibits heme-dependent protein synthesis in Plasmodium falciparum.
• YC-1 activation of human soluble guanylyl cyclase has both heme-dependent and heme-independent components
• Proteome Analyses of Heme-Dependent Respiration in Lactococcus lactis: Involvement of the Proteolytic System
• The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species.