Paradoxical effects of methylmercury on the kinetics of cytochrome c oxidase
David Bickar, Michael T. Wilson(University of Essex), Henry Auer, Celia Bonaventura(Duke University), Joseph Bonaventura(University of Essex)
Cited by 9
Related Papers
Blood Flow Regulation by <i>S</i> -Nitrosohemoglobin in the Physiological Oxygen Gradient
|Science|1997|1.1k
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
|Proteins Structure Function and Bioinformatics|1994|397
Crystal structure of deoxygenated <i>limulus polyphemus</i> subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation
|Protein Science|1993|307
Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome <i>c</i> oxidase
|Proceedings of the National Academy of Sciences|2006|232