Ontology highlight
ABSTRACT:
SUBMITTER: Tanaka M
PROVIDER: S-EPMC139504 | biostudies-literature | 2002 Feb
REPOSITORIES: biostudies-literature
Journal of bacteriology 20020201 3
A cytochrome in an extremely halophilic archaeon, Haloferax volcanii, was purified to homogeneity. This protein displayed a redox difference spectrum that is characteristic of a-type cytochromes and a CN(-) complex spectrum that indicates the presence of heme a and heme a(3). This cytochrome aa(3) consisted of 44- and 35-kDa subunits. The amino acid sequence of the 44-kDa subunit was similar to that of the heme-copper oxidase subunit I, and critical amino acid residues for metal binding, such as ...[more]