The octahaem MccA is a haem c-copper sulfite reductase

Nature

Volumn 520, Issue 7549, 2015, Pages 706-709

  Hermann, Bianca ^a   Kern, Melanie ^b   La Pietra, Luigi ^b   Simon, Jörg ^b   Einsle, Oliver ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ION; CYTOCHROME C; HEME; IRON; METAL; NITRITE; SULFITE; SULFITE REDUCTASE; SULFUR DIOXIDE; BACTERIAL PROTEIN; COPPER; CYSTEINE; CYSTEINE THIOLATE; HEME C; OXIDOREDUCTASE;

BIOGEOCHEMICAL CYCLE; CATALYSIS; COPPER; DEHYDRATION; ELECTRON; ENZYME ACTIVITY; PURIFICATION; REDOX POTENTIAL; SULFITE; SULFUR DIOXIDE; WAVELENGTH;

ARTICLE; BACTERIUM; BIOGEOCHEMICAL CYCLE; CATALYSIS; DEHYDRATION; DISPERSION; ENZYME ACTIVE SITE; ENZYME ISOLATION; ENZYME STRUCTURE; NONHUMAN; OXIDATION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN MOTIF; X IRRADIATION; ANALOGS AND DERIVATIVES; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; OXIDATION REDUCTION REACTION; WOLINELLA; X RAY CRYSTALLOGRAPHY;

SEIRA;

BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; COPPER; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; HEME; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON SULFUR GROUP DONORS; SULFITES; SULFUR DIOXIDE; WOLINELLA;

EID: 84928819631     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14109     Document Type: Article

References (37)

1. Simon, J. & Kroneck, P. M. H. Microbial sulfite respiration. Adv. Microb. Physiol. 62, 45-117 (2013).
2. Kern, M., Klotz, M. G. & Simon, J. The Wolinella succinogenes mcc gene cluster encodes an unconventional respiratory sulphite reduction system. Mol. Microbiol. 82, 1515-1530 (2011).
3. Hartshorne, R. S. et al. A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding. Mol. Microbiol. 64, 1049-1060 (2007).
4. Lukat, P. et al. Binding and reduction of sulfite by cytochrome c nitrite reductase. Biochemistry 47, 2080-2086 (2008).
5. Kemp, G. L. et al. Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coil. Biochem. J. 431, 73-80 (2010).
6. Pereira, I. A. C., LeGall, J., Xavier, A. V. & Teixeira, M. Characterization of a heme c nitrite reductase from a non-ammonifying microorganism, Desulfovibrio vulgaris Hildenborough. Biochim. Biophys. Acta 1481, 119-130 (2000).
7. Steuber, J., Arendsen, A. F., Hagen, W. R.&Kroneck, P. M. H. Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans Essex and comparison with the enzyme from Desulfovibrio vulgaris Hildenborough. Eur. J. Biochem. 233, 873-879 (1995).
8. Shirodkar, S., Reed, S., Romine, M. & Saffarini, D. The octahaem SirA catalyses dissimilatory sulfite reduction in Shewanella oneidensis MR-1. Environ. Microbiol. 13, 108-115 (2011).
9. Klotz, M. G. et al. Evolution of an octahaem cytochrome c protein family that is key to aerobic and anaerobic ammonia oxidation by bacteria. Environ. Microbiol. 10, 3150-3163 (2008).
10. Einsle, O. et al. Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1. 6A? resolution, inhibitor binding, and heme-packing motifs. J. Biol. Chem. 275, 39608-39616 (2000).
11. Iverson, T. M. et al. Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nature Struct. Biol. 5, 1005-1012 (1998).
12. Einsle, O. Structure and function of formate-dependent cytochrome c nitrite reductase, NrfA. Methods Enzymol. 496, 399-422 (2011).
13. Einsle, O. et al. Structure of cytochrome c nitrite reductase. Nature 400, 476-480 (1999).
14. Igarashi, N., Moriyama, H., Fujiwara, T., Fukumori, Y. & Tanaka, N. The 2. 8A? structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nature Struct. Biol. 4, 276-284 (1997).
15. Polyakov, K. M. et al. High-resolution structural analysis of a novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacteriumThioalkalivibrio nitratireducens. J. Mol. Biol. 389, 846-862 (2009).
16. Mowat, C. G. et al. Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nature Struct. Mol. Biol. 11, 1023-1024 (2004).
17. Hartshorne, S., Richardson, D. J. & Simon, J. Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis. Biochem. Soc. Trans. 34, 146-149 (2006).
18. Kern, M., Eisel, F., Scheithauer, J., Kranz, R. G. & Simon, J. Substrate specificity of three cytochrome c haem lyase isoenzymes from Wolinella succinogenes: unconventional haemc bindingmotifs are not sufficient for haemc attachment by Nrfl and CcsA1. Mol. Microbiol. 75, 122-137 (2010).
19. Simon, J. & Hederstedt, L. Composition and function of cytochrome c biogenesis System II. FEBS J. 278, 4179-4188 (2011).
20. Aoyama, H. et al. A peroxide bridge between Fe and Cu ions in theO2 reduction site of fully oxidized cytochromec oxidase could suppress the proton pump. Proc. Natl Acad. Sci. USA 106, 2165-2169 (2009).
21. Schiffer, A. et al. Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus. J. Mol. Biol. 379, 1063-1074 (2008).
22. Kern, M. & Simon, J. Production of recombinant multiheme cytochromes c in Wolinella succinogenes. Methods Enzymol. 486, 429-446 (2011).
23. Kabsch, W. XDS. Acta Crystallogr. D 66, 125-132 (2010).
24. Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D 69, 1204-1214 (2013).
25. Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235-242 (2011).
26. Sheldrick, G. M. A short history of SHELX. Acta Crystallogr. A 64, 112-122 (2008).
27. Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M. & Paciorek, W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2. 0. Acta Crystallogr. D 59, 2023-2030 (2003).
28. Vonrhein, C., Blanc, E., Roversi, P.&Bricoone, G. Automated structure solution with autoSHARP. Methods Mol. Biol. 364, 215-230 (2007).
29. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486-501 (2010).
30. Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355-367 (2011).
31. Vagin, A. & Teplyakov, A. Molecular replacement with MOLREP. Acta Crystallogr. D 66, 22-25 (2010).
32. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
33. Cedervall, P., Hooper, A. B. & Wilmot, C. M. Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner. Biochemistry 52, 6211-6218 (2013).
34. Weiss, M. & Hilgenfeld, R. On the use of the merging R factor as a quality indicator for X-ray data. J. Appl. Cryst. 30, 203-205 (1997).
35. Karplus, P. A. & Diederichs, K. Linking crystallographic model and data quality. Science 336, 1030-1033 (2012).
36. Cruickshank, D. W. J. Remarks about protein structure precision. Acta Crystallogr. D 55, 583-601 (1999).
37. Bru?ger, A. T. FreeR value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).