Characterization of Electron Transfer Proteins

1995 ◽  
pp. 113-149 ◽  
Author(s):  
Liang Chen ◽  
Ming-Y. Liu ◽  
Jean Le Gall
Keyword(s):  
Electron Transfer ◽  
Electron Transfer Proteins

Characterization of an Operon Encoding Two c-Type Cytochromes, an aa3-Type Cytochrome Oxidase, and Rusticyanin in Thiobacillus ferrooxidansATCC 33020

1999 ◽  
Vol 65 (11) ◽  
pp. 4781-4787 ◽  
Author(s):  
Corinne Appia-Ayme ◽  
Nicolas Guiliani ◽  
Jeanine Ratouchniak ◽  
Violaine Bonnefoy
Keyword(s):  
Electron Transfer ◽  
Thiobacillus Ferrooxidans ◽  
Energetic Metabolism ◽  
Reading Frame ◽  
Electron Transfer Proteins ◽  
Reverse Transcription Pcr ◽  
Genes Encoding ◽  
Transcriptional Start Sites ◽  
Transfer Chain

ABSTRACT Despite the importance of Thiobacillus ferrooxidans in bioremediation and bioleaching, little is known about the genes encoding electron transfer proteins implicated in its energetic metabolism. This paper reports the sequences of the fourcox genes encoding the subunits of anaa 3-type cytochrome c oxidase. These genes are in a locus containing four other genes:cyc2, which encodes a high-molecular-weight cytochromec; cyc1, which encodes ac 4-type cytochrome (c 552); open reading frame 1, which encodes a putative periplasmic protein of unknown function; and rus, which encodes rusticyanin. The results of Northern and reverse transcription-PCR analyses indicated that these eight genes are cotranscribed. Two transcriptional start sites were identified for this operon. Upstream from each of the start sites was a ς70-type promoter recognized in Escherichia coli. While transcription in sulfur-grown T. ferrooxidans cells was detected from the two promoters, transcription in ferrous-iron-grown T. ferrooxidans cells was detected only from the downstream promoter. The cotranscription of seven genes encoding redox proteins suggests that all these proteins are involved in the same electron transfer chain; a model taking into account the biochemistry and the genetic data is discussed.

Characterization of electron transfer proteins from the nitrogen-fixing sulphate-reducing bacterium Desulfovibrio desulfuricans Berre-Eau

1987 ◽  
Vol 15 (6) ◽  
pp. 1049-1050
Author(s):  
GUY FAUQUE ◽  
ISABEL MOURA ◽  
ANTONIO V. XAVIER ◽  
NICOLE GALLIANO ◽  
JOSÉ J. G. MOURA ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Desulfovibrio Desulfuricans ◽  
Nitrogen Fixing ◽  
Electron Transfer Proteins

Isolation and Characterization of Soluble Electron Transfer Proteins fromChromatium purpuratum†

Biochemistry ◽  
1996 ◽  
Vol 35 (24) ◽  
pp. 7812-7818 ◽  
Author(s):  
Cheryl A. Kerfeld ◽  
Cheryl Chan ◽  
Masakazu Hirasawa ◽  
Susan Kleis-SanFrancisco ◽  
Todd O. Yeates ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Electron Transfer Proteins ◽  
Isolation And Characterization

Synthesis and Characterization of C70-Corrole—A New Electron Transfer Dyad

2014 ◽  
Vol 14 (7) ◽  
pp. 5370-5374 ◽  
Author(s):  
Youde Wang ◽  
Zhenzhen Wang ◽  
Xihong Guo ◽  
Rongli Cui ◽  
Xingfa Gao ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Synthesis And Characterization

scholarly journals Characterization of P450 FcpC, the Enzyme Responsible for Bioconversion of Diosgenone to Isonuatigenone in Streptomyces virginiae IBL-14

2009 ◽  
Vol 75 (12) ◽  
pp. 4202-4205 ◽  
Author(s):  
Wei Wang ◽  
Feng-Qing Wang ◽  
Dong-Zhi Wei
Keyword(s):  
Escherichia Coli ◽  
Electron Transfer ◽  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Whole Cell ◽  
Electron Transfer Chain ◽  
Streptomyces Virginiae ◽  
Transfer Chain

ABSTRACT A new cytochrome P450 monooxygenase, FcpC, from Streptomyces virginiae IBL-14 has been identified. This enzyme is found to be responsible for the bioconversion of a pyrano-spiro steroid (diosgenone) to a rare nuatigenin-type spiro steroid (isonuatigenone), which is a novel C-25-hydroxylated diosgenone derivative. A whole-cell P450 system was developed for the production of isonuatigenone via the expression of the complete three-component electron transfer chain in an Escherichia coli strain.

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