1lm2

NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7

spinqualitylabelsall models 1lm2, 35 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lm2 is a 1 chain structure with sequence from Desulfuromonas acetoxidans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CR, HEC Related: 1new, 2new, 1ehj, 1hh5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [CYC3_DESAC] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The redox reaction between CrO(4)(2-) and the fully reduced three-heme cytochrome c(7) from Desulfuromonas acetoxidans to give chromium(III) and the fully oxidized protein has been followed by NMR spectroscopy. The hyperfine coupling between the oxidized protein protons and chromium(III), which remains bound to the protein, gives rise to line-broadening effects on the NMR resonances that can be transformed into proton-metal distance restraints. Structure calculations based on these unconventional constraints allowed us to demonstrate that chromium(III) binds at a unique site and to locate it on the protein surface. The metal ion is located 7.9 +/- 0.4 A from the iron of heme IV, 16.3 +/- 0.7 A from the iron of heme III, and 22.5 +/- 0.5 A from the iron of heme I. Shift changes caused by the presence of unreactive MoO(4)(2-), a CrO(4)(2-) analogue, indicate the involvement of the same protein area in the anion binding. The titration of the oxidation of cytochrome c(7) shows a detailed mechanism of action. The presence of a specific binding site supports the hypothesis of the biological role of this cytochrome as a metal reductase. The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7).,Assfalg M, Bertini I, Bruschi M, Michel C, Turano P Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9750-4. Epub 2002 Jul 15. PMID:12119407 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c Cytochrome c 7

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