scholarly journals NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase.

1993 ◽  
Vol 268 (25) ◽  
pp. 18604-18609
Author(s):  
J. Covès ◽  
V. Nivière ◽  
M. Eschenbrenner ◽  
M. Fontecave
Keyword(s):  
Escherichia Coli ◽  
Free Radical ◽  
Ribonucleotide Reductase ◽  
Sulfite Reductase ◽  
Flavin Reductase

An ENDOR study of the tyrosyl free radical in ribonucleotide reductase from Escherichia coli

1989 ◽  
Vol 111 (21) ◽  
pp. 8076-8083 ◽  
Author(s):  
Christopher J. Bender ◽  
Margareta Sahlin ◽  
Gerald T. Babcock ◽  
Bridgette A. Barry ◽  
T. K. Chandrashekar ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Free Radical ◽  
Ribonucleotide Reductase

scholarly journals The tyrosine free radical in ribonucleotide reductase from Escherichia coli.

1978 ◽  
Vol 253 (19) ◽  
pp. 6863-6865 ◽  
Author(s):  
B.M. Sjöberg ◽  
P. Reichard ◽  
A. Gräslund ◽  
A. Ehrenberg
Keyword(s):  
Escherichia Coli ◽  
Free Radical ◽  
Ribonucleotide Reductase

scholarly journals Role for CysJ Flavin Reductase in Molybdenum Cofactor-Dependent Resistance of Escherichia coli to 6-N-Hydroxylaminopurine

2010 ◽  
Vol 192 (8) ◽  
pp. 2026-2033 ◽  
Author(s):  
Stanislav G. Kozmin ◽  
Jian Wang ◽  
Roel M. Schaaper
Keyword(s):  
Escherichia Coli ◽  
Reductase Activity ◽  
Molybdenum Cofactor ◽  
Sulfite Reductase ◽  
Flavin Reductase ◽  
Additional Component ◽  
E Coli ◽  
Base Analog ◽  
Related Compounds

ABSTRACT We have previously described a novel Escherichia coli detoxification system for the removal of toxic and mutagenic N-hydroxylated nucleobases and related compounds that requires the molybdenum cofactor. Two subpathways (ycbX and yiiM) were identified, each employing a novel molybdo activity capable of inactivating N-hydroxylated compounds by reduction to the corresponding amine. In the present study, we identify the cysJ gene product as one additional component of this system. While the CysJ protein has been identified as the NADPH:flavin oxidoreductase component of the CysJI sulfite reductase complex (CysJ8I4), we show that the role of CysJ in base analog detoxification is unique and independent of CysI and sulfite reductase. We further show that CysJ functions as a specific partner of the YcbX molybdoenzyme. We postulate that the function of CysJ in this pathway is to provide, via its NADPH:flavin reductase activity, the reducing equivalents needed for the detoxification reaction at the YcbX molybdocenter. In support of the proposed interaction of the CysJ and YcbX proteins, we show that an apparent CysJ-YcbX “hybrid” protein from two Vibrio species is capable of compensating for a double cysJ ycbX defect in E. coli.

The Free Radical in Ribonucleotide Reductase from Escherichia coli

1977 ◽  
Vol 5 (3) ◽  
pp. 747-748
Author(s):  
BRITT-MARIE SJÖBERG ◽  
ASTRID GRÄSLUND
Keyword(s):  
Escherichia Coli ◽  
Free Radical ◽  
Ribonucleotide Reductase
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