Conformational change accompanies redox reactions of the tetraheme cytochrome c-554 of Nitrosomonas europaea
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1987.tb10600.x/fullpdf
Reference23 articles.
1. Cytochrome c554 as a possible electron donor in the hydroxylation of ammonia and carbon monoxide in Nitrosomonas europaea
2. O2and H2O are each the source of one O in NO−2produced from NH3byNitrosomonas:15N-NMR evidence
3. Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and optical spectroscopy
4. 4. A. B. Hooper, W. R. Strohl, and O. H. Tuovinen (1984 ) inMicrobial chemoautotrophy () pp.133 -167 , Ohio State University Press, Columbus OH.
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1. Cytochromec554;Encyclopedia of Inorganic and Bioinorganic Chemistry;2011-12-15
2. Direct Electrochemistry of Tetraheme Cytochrome c554 from Nitrosomonas europaea: Redox Cooperativity and Gating;Journal of the American Chemical Society;2007-01-31
3. Cytochromec554;Handbook of Metalloproteins;2006-04-15
4. NO Reductase Activity of the Tetraheme Cytochrome c554 of Nitrosomonas europaea;Journal of the American Chemical Society;2006-03-10
5. Kinetics of Dithionite-Dependent Reduction of Cytochrome P450 3A4: Heterogeneity of the Enzyme Caused by Its Oligomerization;Biochemistry;2005-09-29
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