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Cytochrome aa(3) in Haloferax volcanii.


ABSTRACT: 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 histidines, were highly conserved. The reduced cytochrome c partially purified from the bacterial membrane fraction was oxidized by the cytochrome aa(3), providing physiological evidence for electron transfer from cytochrome c to cytochrome aa(3) in archaea.

SUBMITTER: Tanaka M 

PROVIDER: S-EPMC139504 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature

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Cytochrome aa(3) in Haloferax volcanii.

Tanaka Mikiei M   Ogawa Naohide N   Ihara Kunio K   Sugiyama Yasuo Y   Mukohata Yasuo Y  

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]

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