Characterization of a heme-dependent catalase from Methanobrevibacter arboriphilus.
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.
Shima
S
S
Max-Planck-Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, D-35043 Marburg, Germany.
Sordel-Klippert
M
M
Brioukhanov
A
A
Netrusov
A
A
Linder
D
D
Thauer
R K
RK
D000595:Amino Acid Sequence; D002374:Catalase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D017013:Methanobacteriaceae / Q000201:enzymology*; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA
D006418:Heme; D002374:Catalase