3bnh: Difference between revisions

Revision as of 08:53, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bnh.png

Template:STRUCTURE 3bnh

W. succinogenes NrfA Y218F Nitrite ComplexW. succinogenes NrfA Y218F Nitrite Complex

Template:ABSTRACT PUBMED 18201106

About this StructureAbout this Structure

3BNH is a Single protein structure of sequence from Wolinella succinogenes. Full crystallographic information is available from OCA.

ReferenceReference

Binding and Reduction of Sulfite by Cytochrome c Nitrite Reductase(,)., Lukat P, Rudolf M, Stach P, Messerschmidt A, Kroneck PM, Simon J, Einsle O, Biochemistry. 2008 Feb 19;47(7):2080-2086. Epub 2008 Jan 18. PMID:18201106

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OCA

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-'''W. succinogenes NrfA Y218F Nitrite Complex'''
+===W. succinogenes NrfA Y218F Nitrite Complex===
-==Overview==
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-Pentaheme cytochrome c nitrite reductase (ccNiR) catalyzes the six-electron reduction of nitrite to ammonia as the final step in the dissimilatory pathway of nitrate ammonification. It has also been shown to reduce sulfite to sulfide, thus forming the only known link between the biogeochemical cycles of nitrogen and of sulfur. We have found the sulfite reductase activity of ccNiR from Wolinella succinogenes to be significantly smaller than its nitrite reductase activity but still several times higher than the one described for dissimilatory, siroheme-containing sulfite reductases. To compare the sulfite reductase activity of ccNiR with our previous data on nitrite reduction, we determined the binding mode of sulfite to the catalytic heme center of ccNiR from W. succinogenes at a resolution of 1.7 A. Sulfite and nitrite both provide a pair of electrons to form the coordinative bond to the Fe(III) active site of the enzyme, and the oxygen atoms of sulfite are found to interact with the three active site protein residues conserved within the enzyme family. Furthermore, we have characterized the active site variant Y218F of ccNiR that exhibited an almost complete loss of nitrite reductase activity, while sulfite reduction remained unaffected. These data provide a first direct insight into the role of the first sphere of protein ligands at the active site in ccNiR catalysis.
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+{{ABSTRACT_PUBMED_18201106}}
 ==About this Structure==
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