Surprising cofactors in metalloenzymes

Current Opinion in Structural Biology

Volumn 13, Issue 2, 2003, Pages 220-226

  Drennan, Catherine L ^a   Peters, John W ^b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b MONTANA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A SYNTHETASE; CARBON MONOXIDE DEHYDROGENASE; HYDROGENASE; METAL COMPLEX; NITROGENASE;

CATALYST; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DESULFOVIBRIO VULGARIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; REVIEW; RHODOSPIRILLUM RUBRUM; STOICHIOMETRY; STRUCTURE ANALYSIS;

DESULFOVIBRIO; DESULFOVIBRIO VULGARIS; RHODOSPIRILLUM; RHODOSPIRILLUM RUBRUM;

EID: 0037399172     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(03)00038-1     Document Type: Review

References (41)

1. Kim J., Rees D.C. Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science. 257:1992;1677-1682.
2. Kim J., Rees D.C. Crystallographic structure and functional implications of the nitrogenase molybdenum iron protein from Azotobacter vinelandii. Nature. 360:1992;553-560.
3. Mayer S.M., Lawson D.M., Gormal C.A., Roe S.M., Smith B.E. New insights into structure-function relationships in nitrogenase: a 1.6 Å resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein. J. Mol. Biol. 292:1999;871-891.
4. Peters J.W., Stowell M.H.B., Soltis S.M., Finnegan M.G., Johnson M.K., Rees D.C. Redox-dependent structural changes in the nitrogenase P-cluster. Biochemistry. 36:1997;1181-1187.
5. Einsle O., Tezcan F.A., Andrade S.L., Schmid B., Yoshida M., Howard J.B., Rees D.C. Nitrogenase MoFe-protein at 1.16 angstrom resolution: a central ligand in the FeMo-cofactor. Science. 297:2002;1696-1700 This paper describes a high-resolution (1.1 Å) analysis of the MoFe protein of nitrogenase, revealing an additional hexacoordinate light atom (assigned as nitrogen) bonded to six Fe atoms within the central core of the FeMo-cofactor.
6. Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 Å resolution. Science. 282:1998;1853-1858.
7. Nicolet Y., Piras C., Legrand P., Hatchikian C.E., Fontecilla-Camps J.C. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure. 7:1999;13-23.
8. Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science. 293:2001;1264-1265 One of the two available three-dimensional structures of the C-cluster of CODH.
9. Drennan C.L., Heo J., Sintchak M.D., Schreiter E., Ludden P.W. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 98:2001;11973-11978 One of the two available three-dimensional structures of the C-cluster of CODH.
10. Doukov T.I., Iverson T.M., Servalli J., Ragsdale S.W., Drennan C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science. 298:2002;567-572 This paper presents the first structure of an A-cluster of a bifunctional CODH/ACS.
11. Holm R.H. Chemical approaches to bridged biological metal assemblies. Pure Appl. Chem. 67:1995;217.
12. Holm R.H., Kennepohl R., Solomon E.I. Structural and functional aspects of metal sites in biology. Chem. Rev. 96:1996;2239-2314.
13. 4] center. J. Am. Chem. Soc. 120:1998;8767-8776.
14. Lindahl P.A. The Ni-containing carbon monoxide dehydrogenase family: light at the end of the tunnel? Biochemistry. 41:2002;2097-2105.
15. Ragsdale S.W., Kumar M. Ni containing carbon monoxide dehydrogenase/acetyl-CoA synthase. Chem. Rev. 96:1996;2515-2539.
16. Tan G.O., Ensign S.A., Ciurli S., Scott M.J., Hedman B., Holm R.H., Ludden P.W., Korszun Z.R., Stephens P.J., Hodgson K.O. On the structure of the nickel/iron/sulfur center of the carbon monoxide dehydrogenase from Rhodospirillum rubrum: an X-ray absorption spectroscopy study. Proc. Natl. Acad. Sci. U.S.A. 89:1992;4427-4431.
17. 2, as revealed by X-ray structure analysis at 1.4Å resolution. Structure. 7:1999;549-556.
18. Harford C., Sarkar B. Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: metal binding, DNA cleavage, and other properties. Acc. Chem. Res. 30:1997;123-130.
19. Huang W., Jia J., Cummings J., Nelson M., Schneider G., Lindqvist Y. Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. Structure. 5:1997;691-699.
20. Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K., Odaka M., Yohda M., Kamiya N., Endo I. Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. Nat. Struct. Biol. 5:1998;347-351.
21. Seravalli J, Gu W, Tam A, Strauss E, Begley TP, Cramer SP, Ragsdale SW: Functional copper at the acetyl-CoA synthase active site. Proc Natl Acad Sci USA 2003, 10.1073/pnas.0436720100.
22. Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O. Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase at 1.1 Å resolution. Proc. Natl. Acad. Sci. U.S.A. 99:2002;15971-15976.
23. Gencic S., Grahame D.A. Nickel in subunit β of the acetyl-CoA decarbonylase/synthase mulitenzyme complex in methanogens. J. Biol. Chem. 278:2003;6101-6110.
24. Volbeda A., Charon M., Piras C., Hatchikian E.C., Frey M., Fontecilla-Camps J.C. Crystal structure of the nickel-iron hydrogenase form Desulfovibrio gigas. Nature. 373:1995;580-587.
25. Higuchi Y., Yagi T., Yasuoka N. Unusual ligand structure in the Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray crystallographic analysis. Structure. 5:1997;1671-1680.
26. Happe R.P., Roseboom W., Pierik A.J., Albracht S.P., Bagley K.A. Biological activation of hydrogen. Nature. 385:1997;126.
27. Nicolet Y., Lemon B.J., Fontecilla-Camps J.C., Peters J.W. A novel FeS cluster in Fe-only hydrogenases. Trends Biochem. Sci. 25:2000;138-143.
28. Van Der Speck T.M., Arendsen A.F., Happe R.P., Yun S., Bagely K.A., Stufkens D.J., Hagen W.R., Albracht S.P.J. Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy. Eur. J. Biochem. 237:1996;629-634.
29. Nicolet Y., de Lacey A.L., Vernede X., Fernanadez V.M., Hatchikian E.C., Fontecilla-Camps J.C. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J. Am. Chem. Soc. 123:2001;1596-1601.
30. Adams M.W.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta. 1020:1990;115-145.
31. Lemon B.J., Peters J.W. Binding of exogenously added carbon monoxide at the active site of the Fe-only hydrogenase from Clostridium pasteurianum. Biochemistry. 38:1999;12969-12973.
32. 4 face of the FeMo cluster of nitrogenase. Aust. J. Chem. 47:1994;979-990.
33. Mayer S.M., Niehaus W.G., Dean D.R. Reduction of short chain alkynes by a nitrogenase a-70Ala-substituted MoFe protein. Dalt. Trans. 1:2002;802.
34. Craft J.L., Mandimutsira B.S., Fuijita K., Riordan C.G., Brunold T.C. Spectroscopic and computational studies of a Ni+-CO model complex: implications for the acetyl-CoA synthase catalytic mechanism. Inorg. Chem. 42:2003;859-867.
35. Laplaza C.E., Holm R.H. Helix-loop-helix peptides as scaffolds for the construction of bridged metal assemblies in proteins: the spectroscopic A-cluster structure in carbon monoxide dehydrogenase. J. Am. Chem. Soc. 123:2001;10255-10264.
36. Smith J.M., Lachicotte R.J., Pittard K.A., Cundari T.R., Lukat-Rogers G., Rodgers K.R., Holland P.L. Stepwise reduction of dinitrogen bond order by a low-coordinate iron complex. J. Am. Chem. Soc. 123:2001;9222-9223.
37. 2-. J. Am. Chem. Soc. 121:1999;9736-9737.
38. Lyon E.J., Georgakaki I.P., Reibenspies J.H., Darensbourg M.Y. Carbon monoxide and cyanide ligands in a classical organometallic complex model for Fe-only hydrogenase. Angew. Chem. Int. Ed. Engl. 38:1999;3178-3180.
39. Le Cloirec A., Best S.P., Borg S., Davies S.C., Evans D.J., Hughes D.L., Pickett C.J. A di-iron dithiolate possessing structural elements of the carbonyl/cyanide sub-site of the H-centre of Fe-only hydrogenase. Chem. Commun. 1:1999;2285-2286.
40. Guex N., Peitsch M.C. Swiss-model and Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
41. 4] clusters in closed and open alpha subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nat Struct Biol 2003, 10.1038/nsb912.