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1d4e
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(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d4e RCSB], [http://www.ebi.ac.uk/pdbsum/1d4e PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d4e RCSB], [http://www.ebi.ac.uk/pdbsum/1d4e PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FRDA_SHEON FRDA_SHEON]] Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 08:10, 25 December 2014
CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE
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