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The Journal of Biological Chemistry|April 25, 1978
The soluble "high potential" type iron-sulfur protein from mitochondria is aconitaseF J Ruzicka, H Beinert
Science (New York, N.Y.)|August 1, 1997
Iron-sulfur clusters: nature's modular, multipurpose structuresH Beinert, R H Holm, E Münck
Proceedings of the National Academy of Sciences of the United States of America|March 28, 1995
Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA bindingN Khoroshilova, H Beinert, P J Kiley
Proceedings of the National Academy of Sciences of the United States of America|October 1, 1973
Oxidation-reduction potentials of bound iron-sulfur proteins of photosystem IB Ke, R E Hansen, H Beinert
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1999
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiaeB Schilke, C Voisine, H Beinert, et al.
The Journal of Biological Chemistry|August 15, 1997
An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxideM C Kennedy, W E Antholine, H Beinert
The Journal of Biological Chemistry|October 10, 1978
A novel electron paramagnetic resonance signal of "oxygenated" cytochrome c oxidaseR W Shaw, R E Hansen, H Beinert
The Journal of Biological Chemistry|March 10, 1984
Incorporation of [35S]sulfide into the Fe-S cluster of aconitaseM C Kennedy, M H Emptage, H Beinert
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