PURIFICATION OF PARACOCCUS-DENITRIFICANS CYTOCHROME C(552) AND SEQUENCE-ANALYSIS OF THE GENE

被引：48

作者：

TURBA, A ^{[1
]}

JETZEK, M ^{[1
]}

LUDWIG, B ^{[1
]}

机构：

[1] UNIV FRANKFURT,BIOZENTRUM N200,INST BIOCHEM,D-60439 FRANKFURT,GERMANY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1995年 / 231卷 / 01期

关键词：

PEPTIDE SEQUENCE; MEMBRANE-BOUND CYTOCHROME; CYTOCHROME-C OXIDASE; MITOCHONDRIAL ELECTRON TRANSPORT; CYCM-ENCODED MEMBRANE ANCHOR;

D O I：

10.1111/j.1432-1033.1995.tb20695.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes in different branches of their electron transport system. Among the many cytochromes c present in the soil bacterium Paracoccus denitrificans, a membrane-bound cytochrome (c(552)) has been suggested to mediate the electron transport between the cytochrome be, complex and cytochrome-e oxidase [Berry, E. A. and Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have purified this cytochrome from cytoplasmic membranes, and cloned and sequenced its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is highly similar to type-I cytochromes c, its N-terminal part contains a hydrophobic segment providing membrane attachment. In addition, we present immunological evidence for its functional role in respiration.

引用

页码：259 / 265

页数：7

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