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Science 6 October 1995:
Vol. 270. no. 5233, pp. 59 - 67
DOI: 10.1126/science.270.5233.59
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Research Articles

Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions

Brian R. Crane,  Lewis M. Siegel,  Elizabeth D. Getzoff (1)

Fundamental chemical transformations for biogeochemical cycling of sulfur and nitrogen are catalyzed by sulfite and nitrite reductases. The crystallographic structure of Escherichia coli sulfite reductase hemoprotein (SiRHP), which catalyzes the concerted six-electron reductions of sulfite to sulfide and nitrite to ammonia, was solved with multiwavelength anomalous diffraction (MAD) of the native siroheme and Fe(4)S(4) cluster cofactors, multiple isomorphous replacement, and selenomethionine sequence markers. Twofold symmetry within the 64-kilodalton polypeptide generates a distinctive three-domain alpha/beta fold that controls cofactor assembly and reactivity. Homology regions conserved between the symmetry-related halves of SiRHP and among other sulfite and nitrite reductases revealed key residues for stability and function, and identified a sulfite or nitrite reductase repeat (SNiRR) common to a redox-enzyme superfamily. The saddle-shaped siroheme shares a cysteine thiolate ligand with the Fe(4)S(4) cluster and ligates an unexpected phosphate anion. In the substrate complex, sulfite displaces phosphate and binds to siroheme iron through sulfur. An extensive hydrogen-bonding network of positive side chains, water molecules, and siroheme carboxylates activates S-O bonds for reductive cleavage.


B. R. Crane and E. D. Getzoff are in the Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. L. M. Siegel is in the Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
(1) To whom correspondence should be addressed.


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