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Science 21 October 1994:
Vol. 266. no. 5184, pp. 430 - 432
DOI: 10.1126/science.7939681
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Articles

Science, Vol 266, Issue 5184, 430-432
Copyright © 1994 by American Association for the Advancement of Science

articles

The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium

ZW Chen, M Koh, G Van Driessche, JJ Van Beeumen, RG Bartsch, TE Meyer, MA Cusanovich, and FS Mathews

Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.

The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin.


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