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Volumn 1817, Issue 3, 2012, Pages 430-444

High-valent [MnFe] and [FeFe] cofactors in ribonucleotide reductases

Author keywords

Chlamydia; MnFe cofactor; Redox intermediate; Ribonucleotide reductase; X ray absorption spectroscopy

Indexed keywords

DNA; IRON; MANGANESE; METAL; RIBONUCLEOTIDE REDUCTASE;

EID: 84855870391     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.12.008     Document Type: Article
Times cited : (13)

References (130)
  • 1
    • 79953305717 scopus 로고    scopus 로고
    • Class i ribonucleotide reductases: Metallocofactor assembly and repair in vitro and in vivo
    • J.A. Cotruvo Jr., and J. Stubbe Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo Annu. Rev. Biochem. 80 2011 19.11 19.35
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 1911-1935
    • Cotruvo, Jr.J.A.1    Stubbe, J.2
  • 2
    • 57049085691 scopus 로고    scopus 로고
    • The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: Structure, assembly, radical initiation, and evolution
    • J.M. Bollinger Jr., W. Jiang, M.T. Green, and C. Krebs The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution Curr. Opin. Struct. Biol. 18 2008 650 657
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 650-657
    • Bollinger, Jr.J.M.1    Jiang, W.2    Green, M.T.3    Krebs, C.4
  • 3
    • 79951502545 scopus 로고    scopus 로고
    • Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear-an intricate bioinorganic workaround to use different metals for the same reaction
    • M. Högbom Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear-an intricate bioinorganic workaround to use different metals for the same reaction Metallomics 3 2011 110 120
    • (2011) Metallomics , vol.3 , pp. 110-120
    • Högbom, M.1
  • 5
    • 33746370368 scopus 로고    scopus 로고
    • Ribonucleotide reductases
    • DOI 10.1146/annurev.biochem.75.103004.142443
    • P. Nordlund, and P. Reichard Ribonucleotide reductases Annu. Rev. Biochem. 75 2006 681 706 (Pubitemid 44118048)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 681-706
    • Nordlund, P.1    Reichard, P.2
  • 6
    • 33845690880 scopus 로고    scopus 로고
    • Ribonucleotide reductase and the regulation of DNA replication: An old story and an ancient heritage
    • DOI 10.1111/j.1365-2958.2006.05493.x
    • J. Herrick, and B. Sclavi Ribonucleotide reductase and the regulation of DNA replication: an old story and an ancient heritage Mol. Microbiol. 63 2007 22 34 (Pubitemid 44968106)
    • (2007) Molecular Microbiology , vol.63 , Issue.1 , pp. 22-34
    • Herrick, J.1    Sclavi, B.2
  • 7
    • 0036301809 scopus 로고    scopus 로고
    • Ribonucleotide reductases: Divergent evolution of an ancient enzyme
    • DOI 10.1007/s00239-002-2311-7
    • E. Torrents, P. Aloy, I. Gibert, and F. Rodriguez-Trelles Ribonucleotide reductases: divergent evolution of an ancient enzyme J. Mol. Evol. 55 2002 138 152 (Pubitemid 34734778)
    • (2002) Journal of Molecular Evolution , vol.55 , Issue.2 , pp. 138-152
    • Torrents, E.1    Aloy, P.2    Gibert, I.3    Rodriguez-Trelles, F.4
  • 8
    • 0026582672 scopus 로고
    • Ribonucleotide reductase: Regulation, regulation, regulation
    • S.J. Elledge, Z. Zhou, and J.B. Allen Ribonucleotide reductase: regulation, regulation, regulation Trends Biochem. Sci. 17 1992 119 123
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 119-123
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3
  • 9
    • 0023666969 scopus 로고
    • Extended x-ray absorption fine structure studies on the iron-containing subunit of ribonucleotide reductase from Escherichia coli
    • G. Bunker, L. Petersson, B.M. Sjöberg, M. Sahlin, M. Chance, B. Chance, and A. Ehrenberg Extended x-ray absorption fine structure studies on the iron-containing subunit of ribonucleotide reductase from Escherichia coli Biochemistry 26 1987 4708 4716
    • (1987) Biochemistry , vol.26 , pp. 4708-4716
    • Bunker, G.1    Petersson, L.2    Sjöberg, B.M.3    Sahlin, M.4    Chance, M.5    Chance, B.6    Ehrenberg, A.7
  • 11
    • 0034528765 scopus 로고    scopus 로고
    • Cloning and characterization of ribonucleotide reductase from Chlamydia trachomatis
    • DOI 10.1074/jbc.M006367200
    • C. Roshick, E.R. Iliffe-Lee, and G. McClarty Cloning and characterization of ribonucleotide reductase from Chlamydia trachomatis J. Biol. Chem. 275 2000 38111 38119 (Pubitemid 32004936)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 38111-38119
    • Roshick, C.1    Iliffe-Lee, E.R.2    McClarty, G.3
  • 12
    • 3042728737 scopus 로고    scopus 로고
    • The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass
    • DOI 10.1126/science.1098419
    • M. Högbom, P. Stenmark, N. Voevodskaya, G. McClarty, A. Gräslund, and P. Nordlund The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass Science 305 2004 245 248 (Pubitemid 38886738)
    • (2004) Science , vol.305 , Issue.5681 , pp. 245-248
    • Hogbom, M.1    Stenmark, P.2    Voevodskaya, N.3    McClart, G.4    Graslund, A.5    Nordlund, P.6
  • 13
    • 34249939132 scopus 로고    scopus 로고
    • A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase
    • DOI 10.1126/science.1141179
    • W. Jiang, D. Yun, L. Saleh, E.W. Barr, G. Xing, L.M. Hoffart, M.A. Maslak, C. Krebs, and J.M. Bollinger Jr. A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase Science 316 2007 1188 1191 (Pubitemid 46877480)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1188-1191
    • Jiang, W.1    Yun, D.2    Saleh, L.3    Barr, E.W.4    Xing, G.5    Hoffart, L.M.6    Maslak, M.-A.7    Krebs, C.8    Bollinger Jr., J.M.9
  • 16
    • 34548665931 scopus 로고    scopus 로고
    • AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases
    • DOI 10.1021/bi701060g
    • C. Krebs, M.L. Matthews, W. Jiang, and J.M. Bollinger Jr. AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases Biochemistry 46 2007 10413 10418 (Pubitemid 47417237)
    • (2007) Biochemistry , vol.46 , Issue.37 , pp. 10413-10418
    • Krebs, C.1    Matthews, M.L.2    Jiang, W.3    Bollinger Jr., J.M.4
  • 17
    • 65249133078 scopus 로고    scopus 로고
    • A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold
    • C.S. Andersson, and M. Högbom A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold Proc. Natl. Acad. Sci. U. S. A. 106 2009 5633 5638
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5633-5638
    • Andersson, C.S.1    Högbom, M.2
  • 18
    • 77949273908 scopus 로고    scopus 로고
    • The manganese/iron-carboxylate proteins: What is what, where are they, and what can the sequences tell us?
    • M. Högbom The manganese/iron-carboxylate proteins: what is what, where are they, and what can the sequences tell us? J. Biol. Inorg. Chem. 15 2010 339 349
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 339-349
    • Högbom, M.1
  • 19
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • DOI 10.1006/jmbi.1993.1374
    • P. Nordlund, and H. Eklund Structure and function of the Escherichia coli ribonucleotide reductase protein R2 J. Mol. Biol. 232 1993 123 164 (Pubitemid 23245406)
    • (1993) Journal of Molecular Biology , vol.232 , Issue.1 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 20
    • 0030587599 scopus 로고    scopus 로고
    • Crystal structure of reduced protein R2 of ribonucleotide reductase: The structural basis for oxygen activation at a dinuclear iron site
    • DOI 10.1016/S0969-2126(96)00112-8
    • D.T. Logan, X.D. Su, A. Aberg, K. Regnström, J. Hajdu, H. Eklund, and P. Nordlund Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site Structure 4 1996 1053 1064 (Pubitemid 26369771)
    • (1996) Structure , vol.4 , Issue.9 , pp. 1053-1064
    • Logan, D.T.1    Su, X.-D.2    Aberg, A.3    Regnstrom, K.4    Hajdu, J.5    Eklund, H.6    Nordlund, P.7
  • 21
    • 0031796531 scopus 로고    scopus 로고
    • Harnessing free radicals: Formation and function of the tyrosyl radical in ribonucleotide reductase
    • DOI 10.1016/S0968-0004(98)01296-1, PII S0968000498012961
    • J. Stubbe, and P. Riggs-Gelasco Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase Trends Biochem. Sci. 23 1998 438 443 (Pubitemid 28540745)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.11 , pp. 438-443
    • Stubbe, J.1    Riggs-Gelasco, P.2
  • 23
    • 0037150125 scopus 로고    scopus 로고
    • Epr studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/I263C protein R2 double mutant of ribonucleotide reductase from mouse
    • DOI 10.1021/bi012043d
    • A. Adrait, M. Öhrström, A.L. Barra, L. Thelander, and A. Gräslund EPR studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/I263C protein R2 double mutant of ribonucleotide reductase from mouse Biochemistry 41 2002 6510 6516 (Pubitemid 34526018)
    • (2002) Biochemistry , vol.41 , Issue.20 , pp. 6510-6516
    • Adrait, A.1    Ohrstrom, M.2    Barra, A.-L.3    Thelander, L.4    Graslund, A.5
  • 24
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • S. Licht, G.J. Gerfen, and J. Stubbe Thiyl radicals in ribonucleotide reductases Science 271 1996 477 481 (Pubitemid 26044465)
    • (1996) Science , vol.271 , Issue.5248 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 25
    • 0026801085 scopus 로고
    • A model for the role of multiple cysteine residues involved in ribonucleotide reduction: Amazing and still confusing
    • S.S. Mao, T.P. Holler, G.X. Yu, J.M. Bollinger Jr., S. Booker, M.I. Johnston, and J. Stubbe A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing Biochemistry 31 1992 9733 9743
    • (1992) Biochemistry , vol.31 , pp. 9733-9743
    • Mao, S.S.1    Holler, T.P.2    Yu, G.X.3    Bollinger, Jr.J.M.4    Booker, S.5    Johnston, M.I.6    Stubbe, J.7
  • 26
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • DOI 10.1074/jbc.272.25.15661
    • W.A. Prinz, F. Åslund, A. Holmgren, and J. Beckwith The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm J. Biol. Chem. 272 1997 15661 15667 (Pubitemid 27265536)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 27
    • 27644446535 scopus 로고    scopus 로고
    • Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase
    • DOI 10.1515/BC.2005.117
    • M. Bennati, F. Lendzian, M. Schmittel, and H. Zipse Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase Biol. Chem. 386 2005 1007 1022 (Pubitemid 41548733)
    • (2005) Biological Chemistry , vol.386 , Issue.10 , pp. 1007-1022
    • Bennati, M.1    Lendzian, F.2    Schmittel, M.3    Zipse, H.4
  • 28
    • 0022763898 scopus 로고
    • Identification of the stable free radical tyrosine residue in ribonucleotide reductase
    • A. Larsson, and B.M. Sjöberg Identification of the stable free radical tyrosine residue in ribonucleotide reductase EMBO J. 5 1986 2037 2040
    • (1986) EMBO J. , vol.5 , pp. 2037-2040
    • Larsson, A.1    Sjöberg, B.M.2
  • 30
    • 84855679844 scopus 로고    scopus 로고
    • The manganese ion of the heterodinuclear Mn/Fe cofactor in Chlamydia trachomatis ribonucleotide reductase R2c is located at metal position 1
    • 10.1021/ja209678x
    • C.S. Andersson, M. Öhrström, A. Popovic-Bijelic, A. Gräslund, P. Stenmark, and M. Högbom The manganese ion of the heterodinuclear Mn/Fe cofactor in Chlamydia trachomatis ribonucleotide reductase R2c is located at metal position 1 J. Am. Chem. Soc. 2012 10.1021/ja209678x
    • (2012) J. Am. Chem. Soc.
    • Andersson, C.S.1    Öhrström, M.2    Popovic-Bijelic, A.3    Gräslund, A.4    Stenmark, P.5    Högbom, M.6
  • 31
    • 64549154416 scopus 로고    scopus 로고
    • Density functional theory study of the manganese-containing ribonucleotide reductase from Chlamydia trachomatis: Why manganese is needed in the active complex
    • K. Roos, and P.E. Siegbahn Density functional theory study of the manganese-containing ribonucleotide reductase from Chlamydia trachomatis: why manganese is needed in the active complex Biochemistry 48 2009 1878 1887
    • (2009) Biochemistry , vol.48 , pp. 1878-1887
    • Roos, K.1    Siegbahn, P.E.2
  • 32
    • 76749163991 scopus 로고    scopus 로고
    • An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
    • J.A. Cotruvo Jr., and J. Stubbe An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase Biochemistry 49 2010 1297 1309
    • (2010) Biochemistry , vol.49 , pp. 1297-1309
    • Cotruvo, Jr.J.A.1    Stubbe, J.2
  • 33
    • 63249128308 scopus 로고    scopus 로고
    • Redox intermediates of the Mn-Fe site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: An X-ray absorption and EPR study
    • N. Voevodskaya, F. Lendzian, O. Sanganas, A. Grundmeier, A. Gräslund, and M. Haumann Redox intermediates of the Mn-Fe site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study J. Biol. Chem. 284 2009 4555 4566
    • (2009) J. Biol. Chem. , vol.284 , pp. 4555-4566
    • Voevodskaya, N.1    Lendzian, F.2    Sanganas, O.3    Grundmeier, A.4    Gräslund, A.5    Haumann, M.6
  • 34
    • 2442664147 scopus 로고    scopus 로고
    • Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase
    • DOI 10.1021/bi036099e
    • L. Saleh, C. Krebs, B.A. Ley, S. Naik, B.H. Huynh, and J.M. Bollinger Jr. Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase Biochemistry 43 2004 5953 5964 (Pubitemid 38669463)
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 5953-5964
    • Saleh, L.1    Krebs, C.2    Ley, B.A.3    Naik, S.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 35
    • 0030000063 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and nuclear magnetic resonance studies of class I ribonucleotide reductase
    • A. Gräslund, and M. Sahlin Electron paramagnetic resonance and nuclear magnetic resonance studies of class I ribonucleotide reductase Annu. Rev. Biophys. Biomol. Struct. 25 1996 259 286 (Pubitemid 26197500)
    • (1996) Annual Review of Biophysics and Biomolecular Structure , vol.25 , pp. 259-286
    • Graslund, A.1    Sahlin, M.2
  • 36
    • 19244377006 scopus 로고    scopus 로고
    • Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography
    • DOI 10.1021/bi9728811
    • W. Tong, D. Burdi, P. Riggs-Gelasco, S. Chen, D. Edmondson, B.H. Huynh, J. Stubbe, S. Han, A. Arvai, and J. Tainer Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography Biochemistry 37 1998 5840 5848 (Pubitemid 28196735)
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 5840-5848
    • Tong, W.1    Burdi, D.2    Riggs-Gelasco, P.3    Chen, S.4    Edmondson, D.5    Huynh, B.H.6    Stubbe, J.7    Han, S.8    Arvai, A.9    Tainer, J.10
  • 38
    • 34447282627 scopus 로고    scopus 로고
    • High catalytic activity achieved with a mixed manganese-iron site in protein R2 of Chlamydia ribonucleotide reductase
    • DOI 10.1016/j.febslet.2007.06.023, PII S0014579307006722
    • N. Voevodskaya, F. Lendzian, A. Ehrenberg, and A. Gräslund High catalytic activity achieved with a mixed manganese-iron site in protein R2 of chlamydia ribonucleotide reductase FEBS Lett. 581 2007 3351 3355 (Pubitemid 47048174)
    • (2007) FEBS Letters , vol.581 , Issue.18 , pp. 3351-3355
    • Voevodskaya, N.1    Lendzian, F.2    Ehrenberg, A.3    Graslund, A.4
  • 39
    • 33645219974 scopus 로고    scopus 로고
    • Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by X-ray irradiation at 10-300 K
    • DOI 10.1074/jbc.M509724200
    • M. Grabolle, M. Haumann, C. Müller, P. Liebisch, and H. Dau Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by X-ray irradiation at 10-300 K J. Biol. Chem. 281 2006 4580 4588 (Pubitemid 43847716)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 4580-4588
    • Grabolle, M.1    Haumann, M.2    Muller, C.3    Liebisch, P.4    Dau, H.5
  • 41
    • 13844294471 scopus 로고    scopus 로고
    • X-ray crystallography and biological metal centers: Is seeing believing?
    • DOI 10.1021/ic0485256
    • M. Sommerhalter, R.L. Lieberman, and A.C. Rosenzweig X-ray crystallography and biological metal centers: is seeing believing? Inorg. Chem. 44 2005 770 778 (Pubitemid 40255947)
    • (2005) Inorganic Chemistry , vol.44 , Issue.4 , pp. 770-778
    • Sommerhalter, M.1    Lieberman, R.L.2    Rosenzweig, A.C.3
  • 42
    • 0000774586 scopus 로고
    • Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes
    • H.H. Thorp Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes Inorg. Chem. 31 1992 1585 1588
    • (1992) Inorg. Chem. , vol.31 , pp. 1585-1588
    • Thorp, H.H.1
  • 43
    • 53249119007 scopus 로고    scopus 로고
    • Biological X-ray absorption spectroscopy (BioXAS): A valuable tool for the study of trace elements in the life sciences
    • R.W. Strange, and M.C. Feiters Biological X-ray absorption spectroscopy (BioXAS): a valuable tool for the study of trace elements in the life sciences Curr. Opin. Struct. Biol. 18 2008 609 616
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 609-616
    • Strange, R.W.1    Feiters, M.C.2
  • 44
    • 38049016877 scopus 로고    scopus 로고
    • The manganese complex of photosystem ii in its reaction cycle-basic framework and possible realization at the atomic level
    • H. Dau, and M. Haumann The manganese complex of photosystem ii in its reaction cycle-basic framework and possible realization at the atomic level Coord. Chem. Rev. 252 2008 273 295
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 273-295
    • Dau, H.1    Haumann, M.2
  • 45
    • 78449282923 scopus 로고    scopus 로고
    • X-ray absorption spectroscopies: Useful tools to understand metallorganic frameworks structure and reactivity
    • S. Bordiga, F. Bonino, K.P. Lillerud, and C. Lamberti X-ray absorption spectroscopies: useful tools to understand metallorganic frameworks structure and reactivity Chem. Soc. Rev. 39 2010 4885 4927
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 4885-4927
    • Bordiga, S.1    Bonino, F.2    Lillerud, K.P.3    Lamberti, C.4
  • 46
    • 57049098226 scopus 로고    scopus 로고
    • Structural analysis of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations
    • J.M. Younker, C.M. Krest, W. Jiang, C. Krebs, J.M. Bollinger Jr., and M.T. Green Structural analysis of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations J. Am. Chem. Soc. 130 2008 15022 15027
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15022-15027
    • Younker, J.M.1    Krest, C.M.2    Jiang, W.3    Krebs, C.4    Bollinger, Jr.J.M.5    Green, M.T.6
  • 48
    • 0030857696 scopus 로고    scopus 로고
    • EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganese-substituted ribonucleotide reductase and hemerythrin
    • DOI 10.1021/bi9702795
    • T.L. Stemmler, T.M. Sossong Jr., J.I. Goldstein, D.E. Ash, T.E. Elgren, D.M. Kurtz Jr., and J.E. Penner-Hahn EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganese-substituted ribonucleotide reductase and hemerythrin Biochemistry 36 1997 9847 9858 (Pubitemid 27364696)
    • (1997) Biochemistry , vol.36 , Issue.32 , pp. 9847-9858
    • Stemmler, T.L.1    Sossong Jr., T.M.2    Goldstein, J.I.3    Ash, D.E.4    Elgren, T.E.5    Kurtz Jr., D.M.6    Penner-Hahn, J.E.7
  • 49
    • 0032506972 scopus 로고    scopus 로고
    • EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor
    • DOI 10.1021/ja9718230
    • P.J. Riggs-Gelasco, L.J. Shu, S.X. Chen, D. Burdi, B.H. Huynh, L. Que, and J. Stubbe EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor J. Am. Chem. Soc. 120 1998 849 860 (Pubitemid 28089880)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.5 , pp. 849-860
    • Riggs-Gelasco, P.J.1
  • 50
    • 0242667931 scopus 로고    scopus 로고
    • Structural Characterization of the Peroxodiiron(III) Intermediate Generated during Oxygen Activation by the W48A/D84E Variant of Ribonucleotide Reductase Protein R2 from Escherichia coli
    • DOI 10.1021/bi035198p
    • J. Baldwin, C. Krebs, L. Saleh, M. Stelling, B.H. Huynh, J.M. Bollinger, and P. Riggs-Gelasco Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli Biochemistry 42 2003 13269 13279 (Pubitemid 37420680)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13269-13279
    • Baldwin, J.1    Krebs, C.2    Saleh, L.3    Stelling, M.4    Huynh, B.H.5    Bollinger Jr., J.M.6    Riggs-Gelasco, P.7
  • 51
    • 0025829053 scopus 로고
    • Purification and characterization of recombinant mouse and herpes-simplex virus ribonucleotide reductase R2 subunit
    • G.J. Mann, A. Gräslund, E.I. Ochiai, R. Ingemarson, and L. Thelander Purification and characterization of recombinant mouse and herpes-simplex virus ribonucleotide reductase R2 subunit Biochemistry 30 1991 1939 1947
    • (1991) Biochemistry , vol.30 , pp. 1939-1947
    • Mann, G.J.1    Gräslund, A.2    Ochiai, E.I.3    Ingemarson, R.4    Thelander, L.5
  • 52
    • 42049105952 scopus 로고    scopus 로고
    • Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide
    • DOI 10.1021/bi702085z
    • W. Jiang, J. Xie, H. Norgaard, J.M. Bollinger Jr., and C. Krebs Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide Biochemistry 47 2008 4477 4483 (Pubitemid 351522097)
    • (2008) Biochemistry , vol.47 , Issue.15 , pp. 4477-4483
    • Jiang, W.1    Xie, J.2    Norgaard, H.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 54
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • DOI 10.1016/j.jmr.2005.08.013, PII S1090780705002892
    • S. Stoll, and A. Schweiger EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178 2006 42 55 (Pubitemid 41774010)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.1 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 56
    • 66649106058 scopus 로고    scopus 로고
    • The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy
    • S. Stripp, O. Sanganas, T. Happe, and M. Haumann The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy Biochemistry 48 2009 5042 5049
    • (2009) Biochemistry , vol.48 , pp. 5042-5049
    • Stripp, S.1    Sanganas, O.2    Happe, T.3    Haumann, M.4
  • 57
    • 13644271567 scopus 로고    scopus 로고
    • 0) characterized by X-ray absorption spectroscopy at 20 K and room temperature
    • DOI 10.1021/bi048697e
    • M. Haumann, C. Muller, P. Liebisch, L. Iuzzolino, J. Dittmer, M. Grabolle, T. Neisius, W. Meyer-Klaucke, and H. Dau Structural and oxidation state changes of the photosystem II manganese complex in four transitions of the water oxidation cycle (S0 -> S1, S1 -> S2, S2 -> S3, and S3,4 -> S0) characterized by X-ray absorption spectroscopy at 20 K and room temperature Biochemistry 44 2005 1894 1908 (Pubitemid 40227473)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 1894-1908
    • Haumann, M.1    Muller, C.2    Liebisch, P.3    Iuzzolino, L.4    Dittmer, J.5    Grabolle, M.6    Neisius, T.7    Meyer-Klaucke, W.8    Dau, H.9
  • 58
    • 0141780871 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy to analyze nuclear geometry and electronic structure of biological metal centers-potential and questions examined with special focus on the tetra-nuclear manganese complex of oxygenic photosynthesis
    • DOI 10.1007/s00216-003-1982-2
    • H. Dau, P. Liebisch, and M. Haumann X-ray absorption spectroscopy to analyze nuclear geometry and electronic structure of biological metal centers-potential and questions examined with special focus on the tetra-nuclear manganese complex of oxygenic photosynthesis Anal. Bioanal. Chem. 376 2003 562 583 (Pubitemid 40882966)
    • (2003) Analytical and Bioanalytical Chemistry , vol.376 , Issue.5 , pp. 562-583
    • Dau, H.1    Liebisch, P.2    Haumann, M.3
  • 60
    • 33750147036 scopus 로고    scopus 로고
    • Theory and calculations of X-ray spectra: XAS, XES, XRS, and NRIXS
    • DOI 10.1016/j.radphyschem.2005.11.014, PII S0969806X06002167
    • J.J. Rehr Theory and calculations of X-ray spectra: XAS, XES, XRS, and NRIXS Radiat. Phys. Chem. 75 2006 1547 1558 (Pubitemid 44602462)
    • (2006) Radiation Physics and Chemistry , vol.75 , Issue.11 SPEC. ISSUE , pp. 1547-1558
    • Rehr, J.J.1
  • 62
    • 77956512545 scopus 로고    scopus 로고
    • Ligand identification in titanium complexes using X-ray valence-to-core emission spectroscopy
    • J.C. Swarbrick, Y. Kvashnin, K. Schulte, K. Seenivasan, C. Lamberti, and P. Glatzel Ligand identification in titanium complexes using X-ray valence-to-core emission spectroscopy Inorg. Chem. 49 2010 8323 8332
    • (2010) Inorg. Chem. , vol.49 , pp. 8323-8332
    • Swarbrick, J.C.1    Kvashnin, Y.2    Schulte, K.3    Seenivasan, K.4    Lamberti, C.5    Glatzel, P.6
  • 64
    • 77955923315 scopus 로고    scopus 로고
    • The CTM4XAS program for EELS and XAS spectral shape analysis of transition metal L-edges
    • E. Stavitski, and F.M. de Groot The CTM4XAS program for EELS and XAS spectral shape analysis of transition metal L-edges Micron 41 2010 687 694
    • (2010) Micron , vol.41 , pp. 687-694
    • Stavitski, E.1    De Groot, F.M.2
  • 65
    • 0000056384 scopus 로고
    • Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes.2. Refined distances and other enzymes
    • W.T. Liu, and H.H. Thorp Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes.2. Refined distances and other enzymes Inorg. Chem. 32 1993 4102 4105
    • (1993) Inorg. Chem. , vol.32 , pp. 4102-4105
    • Liu, W.T.1    Thorp, H.H.2
  • 66
    • 0001686483 scopus 로고    scopus 로고
    • Bond valence sums in coordination chemistry using oxidation state independent R-0 values. A simple method for calculating the oxidation state of manganese in complexes containing only Mn-O bonds
    • G.J. Palenik Bond valence sums in coordination chemistry using oxidation state independent R-0 values. A simple method for calculating the oxidation state of manganese in complexes containing only Mn-O bonds Inorg. Chem. 36 1997 4888 4890
    • (1997) Inorg. Chem. , vol.36 , pp. 4888-4890
    • Palenik, G.J.1
  • 67
    • 0004473925 scopus 로고    scopus 로고
    • Bond valence sums in coordination chemistry. A simple method for calculating the oxidation state of cobalt in complexes containing only Co-O bonds
    • R.M. Wood, and G.J. Palenik Bond valence sums in coordination chemistry. A simple method for calculating the oxidation state of cobalt in complexes containing only Co-O bonds Inorg. Chem. 37 1998 4149 4151
    • (1998) Inorg. Chem. , vol.37 , pp. 4149-4151
    • Wood, R.M.1    Palenik, G.J.2
  • 70
    • 84856495225 scopus 로고    scopus 로고
    • Orca: An ab-initio, DFT, and semiempirical electronic structure package. V.2.6.35
    • University of Bonn Bonn, Germany
    • F. Neese Orca: an ab-initio, DFT, and semiempirical electronic structure package. V.2.6.35 Theoretical Chemistry Group 2008 University of Bonn Bonn, Germany
    • (2008) Theoretical Chemistry Group
    • Neese, F.1
  • 71
    • 79953130211 scopus 로고    scopus 로고
    • Carboxylate shifts steer interquinone electron transfer in photosynthesis
    • P. Chernev, I. Zaharieva, H. Dau, and M. Haumann Carboxylate shifts steer interquinone electron transfer in photosynthesis J. Biol. Chem. 286 2011 5368 5374
    • (2011) J. Biol. Chem. , vol.286 , pp. 5368-5374
    • Chernev, P.1    Zaharieva, I.2    Dau, H.3    Haumann, M.4
  • 72
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • A.D. Becke Density-functional exchange-energy approximation with correct asymptotic behavior Phys. Rev. A 38 1988 3098
    • (1988) Phys. Rev. A , vol.38 , pp. 3098
    • Becke, A.D.1
  • 73
    • 0039209924 scopus 로고
    • Fully optimized contracted Gaussian basis sets of triple zeta valence quality for atoms Li to Kr
    • A. Schäfer, C. Huber, and R. Ahlrichs Fully optimized contracted Gaussian basis sets of triple zeta valence quality for atoms Li to Kr J. Chem. Phys. 100 1994 5829 5835
    • (1994) J. Chem. Phys. , vol.100 , pp. 5829-5835
    • Schäfer, A.1    Huber, C.2    Ahlrichs, R.3
  • 74
    • 33644589017 scopus 로고    scopus 로고
    • Accurate Coulomb-fitting basis sets for H to Rn
    • F. Weigend Accurate Coulomb-fitting basis sets for H to Rn Phys. Chem. Chem. Phys. 8 2006 1057 1065
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 1057-1065
    • Weigend, F.1
  • 75
    • 84961974101 scopus 로고    scopus 로고
    • Calculation of solvent shifts on electronic g-tensors with the conductor-like screening model (COSMO) and its self-consistent generalization to real solvents (direct COSMO-RS)
    • DOI 10.1021/jp056016z
    • S. Sinnecker, A. Rajendran, A. Klamt, M. Diedenhofen, and F. Neese Calculation of solvent shifts on electronic g-tensors with the conductor-like screening model (COSMO) and its self-consistent generalization to real solvents (direct COSMO-RS) J. Phys. Chem. A 110 2006 2235 2245 (Pubitemid 43342977)
    • (2006) Journal of Physical Chemistry A , vol.110 , Issue.6 , pp. 2235-2245
    • Sinnecker, S.1    Rajendran, A.2    Klamt, A.3    Diedenhofen, M.4    Neese, F.5
  • 76
    • 47049100080 scopus 로고    scopus 로고
    • Magnetic interactions in alkyl substituted cyclohexane diradical systems: A broken symmetry approach
    • P. Seal, and S. Chakrabarti Magnetic interactions in alkyl substituted cyclohexane diradical systems: a broken symmetry approach J. Phys. Chem. A 112 2008 3409 3413
    • (2008) J. Phys. Chem. A , vol.112 , pp. 3409-3413
    • Seal, P.1    Chakrabarti, S.2
  • 77
    • 1542366648 scopus 로고    scopus 로고
    • IV Model Compound
    • DOI 10.1021/ja0390202
    • S. Sinnecker, F. Neese, L. Noodleman, and W. Lubitz Calculating the electron paramagnetic resonance parameters of exchange coupled transition metal complexes using broken symmetry density functional theory: application to a MnIII/MnIV model compound J. Am. Chem. Soc. 126 2004 2613 2622 (Pubitemid 38295742)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.8 , pp. 2613-2622
    • Sinnecker, S.1    Neese, F.2    Noodleman, L.3    Lubitz, W.4
  • 78
    • 67650092935 scopus 로고    scopus 로고
    • Metal binding and activity of ribonucleotide reductase protein R2 mutants: Conditions for formation of the mixed manganese-iron cofactor
    • A. Popovic-Bijelic, N. Voevodskaya, V. Domkin, L. Thelander, and A. Gräslund Metal binding and activity of ribonucleotide reductase protein R2 mutants: conditions for formation of the mixed manganese-iron cofactor Biochemistry 48 2009 6532 6539
    • (2009) Biochemistry , vol.48 , pp. 6532-6539
    • Popovic-Bijelic, A.1    Voevodskaya, N.2    Domkin, V.3    Thelander, L.4    Gräslund, A.5
  • 80
    • 0000106396 scopus 로고
    • Models for nonheme iron oxygenases-A high-valent iron oxo intermediate
    • R.A. Leising, B.A. Brennan, L. Que, and E. Munck Models for nonheme iron oxygenases-a high-valent iron oxo intermediate J. Am. Chem. Soc. 113 1991 3988 3990
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 3988-3990
    • Leising, R.A.1    Brennan, B.A.2    Que, L.3    Munck, E.4
  • 81
    • 0037007237 scopus 로고    scopus 로고
    • Bis(μ-O)dimetal "diamond" cores in copper and iron complexes relevant to biocatalysis
    • L. Que, and W.B. Tolman Bis(μ-O)dimetal "Diamond" cores in copper and iron complexes relevant to biocatalysis Angew. Chem. Int. Ed Engl. 41 2002 1114 1137
    • (2002) Angew. Chem. Int. Ed Engl. , vol.41 , pp. 1114-1137
    • Que, L.1    Tolman, W.B.2
  • 82
    • 0001557834 scopus 로고
    • Electronic and Raman-spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compounds
    • J. Sanders-Loehr, W.D. Wheeler, A.K. Shiemke, B.A. Averill, and T.M. Loehr Electronic and Raman-spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compounds J. Am. Chem. Soc. 111 1989 8084 8093
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8084-8093
    • Sanders-Loehr, J.1    Wheeler, W.D.2    Shiemke, A.K.3    Averill, B.A.4    Loehr, T.M.5
  • 83
    • 10144241646 scopus 로고
    • Oxo-bridged and hydroxo-bridged diiron complexes-A chemical perspective on a biological unit
    • D.M. Kurtz Oxo-bridged and hydroxo-bridged diiron complexes-a chemical perspective on a biological unit Chem. Rev. 90 1990 585 606
    • (1990) Chem. Rev. , vol.90 , pp. 585-606
    • Kurtz, D.M.1
  • 84
    • 0023653149 scopus 로고
    • Identification of a hydroxide ligand at the iron center of ribonucleotide reductase by resonance Raman spectroscopy
    • B.M. Sjöberg, J. Sanders-Loehr, and T.M. Loehr Identification of a hydroxide ligand at the iron center of ribonucleotide reductase by resonance Raman spectroscopy Biochemistry 26 1987 4242 4247
    • (1987) Biochemistry , vol.26 , pp. 4242-4247
    • Sjöberg, B.M.1    Sanders-Loehr, J.2    Loehr, T.M.3
  • 85
    • 0032552881 scopus 로고    scopus 로고
    • 9 desaturase: Oxidase reactivity during single turnover and implications for the mechanism of desaturation
    • DOI 10.1021/bi981839i
    • J.A. Broadwater, J. Ai, T.M. Loehr, J. Sanders-Loehr, and B.G. Fox Peroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation Biochemistry 37 1998 14664 14671 (Pubitemid 28487574)
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14664-14671
    • Broadwater, J.A.1    Ai, J.2    Loehr, T.M.3    Sanders-Loehr, J.4    Fox, B.G.5
  • 86
    • 0033609131 scopus 로고    scopus 로고
    • The ferroxidase reaction of ferritin reveals a diferric mu-1,2 bridging peroxide intermediate in common with other O-2-activating non-heme diiron proteins
    • P. Moenne-Loccoz, C. Krebs, K. Herlihy, D.E. Edmondson, E.C. Theil, B.H. Huynh, and T.M. Loehr The ferroxidase reaction of ferritin reveals a diferric mu-1,2 bridging peroxide intermediate in common with other O-2-activating non-heme diiron proteins Biochemistry 38 1999 5290 5295
    • (1999) Biochemistry , vol.38 , pp. 5290-5295
    • Moenne-Loccoz, P.1    Krebs, C.2    Herlihy, K.3    Edmondson, D.E.4    Theil, E.C.5    Huynh, B.H.6    Loehr, T.M.7
  • 88
    • 33645846958 scopus 로고    scopus 로고
    • Resonance Raman spectroscopy of oxoiron(IV) porphyrin Pi-cation radical and oxoiron(IV) hemes in peroxidase intermediates
    • J. Terner, V. Palaniappan, A. Gold, R. Weiss, M.M. Fitzgerald, A.M. Sullivan, and C.M. Hosten Resonance Raman spectroscopy of oxoiron(IV) porphyrin Pi-cation radical and oxoiron(IV) hemes in peroxidase intermediates J. Inorg. Biochem. 100 2006 480 501
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 480-501
    • Terner, J.1    Palaniappan, V.2    Gold, A.3    Weiss, R.4    Fitzgerald, M.M.5    Sullivan, A.M.6    Hosten, C.M.7
  • 89
    • 77953906046 scopus 로고    scopus 로고
    • Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: Implications for the protein gating of intersubunit electron transfer
    • W. Jiang, J.J. Xie, P.T. Varano, C. Krebs, and J.M. Bollinger Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer Biochemistry 49 2010 5340 5349
    • (2010) Biochemistry , vol.49 , pp. 5340-5349
    • Jiang, W.1    Xie, J.J.2    Varano, P.T.3    Krebs, C.4    Bollinger, J.M.5
  • 90
    • 0027311206 scopus 로고
    • The dimanganese(III,IV) oxidation state of catalase from Thermus thermophilus: Electron nuclear double resonance analysis of water and protein ligands in the active site
    • DOI 10.1021/bi00069a028
    • S. Khangulov, M. Sivaraja, V.V. Barynin, and G.C. Dismukes The dimanganese(III, IV) oxidation-state of catalase from Thermus thermophilus-electron nuclear double-resonance analysis of water and protein ligands in the active-site Biochemistry 32 1993 4912 4924 (Pubitemid 23162049)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4912-4924
    • Khangulov, S.1    Sivaraja, M.2    Barynin, V.V.3    Dismukes, G.C.4
  • 92
    • 17044390320 scopus 로고    scopus 로고
    • A stable FeIII-FeIV replacement of tyrosyl radical in a class i ribonucleotide reductase
    • N. Voevodskaya, F. Lendzian, and A. Gräslund A stable FeIII-FeIV replacement of tyrosyl radical in a class I ribonucleotide reductase Biochem. Biophys. Res. Commun. 330 2005 1213 1216
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 1213-1216
    • Voevodskaya, N.1    Lendzian, F.2    Gräslund, A.3
  • 93
    • 0001956789 scopus 로고
    • Simulation of the EMR spectra of high-spin iron in proteins
    • L.J.R. Berliner, J. Plenum Press New York
    • B.J.S. Gaffney, and H. J. Simulation of the EMR spectra of high-spin iron in proteins L.J.R. Berliner, J. EMR of Paramagnetic Molecules 1993 Plenum Press New York 1 57
    • (1993) EMR of Paramagnetic Molecules , pp. 1-57
    • Gaffney, B.J.S.1
  • 94
    • 72949122846 scopus 로고    scopus 로고
    • Thioester hydrolysis reactivity of an Fe(III)Zn(II) complex
    • J.J. Danford, P. Dobrowolski, and L.M. Berreau Thioester hydrolysis reactivity of an Fe(III)Zn(II) complex Inorg. Chem. 48 2009 11352 11361
    • (2009) Inorg. Chem. , vol.48 , pp. 11352-11361
    • Danford, J.J.1    Dobrowolski, P.2    Berreau, L.M.3
  • 95
    • 77951189303 scopus 로고    scopus 로고
    • Linear dichroism in the XANES of partially oriented samples: Theory and application to the photosynthetic manganese complex
    • P. Liebisch, and H. Dau Linear dichroism in the XANES of partially oriented samples: theory and application to the photosynthetic manganese complex Chemphyschem 11 2010 1236 1247
    • (2010) Chemphyschem , vol.11 , pp. 1236-1247
    • Liebisch, P.1    Dau, H.2
  • 98
    • 9344248097 scopus 로고    scopus 로고
    • XAS characterization of end-on and side-on peroxoiron(III) complexes of the neutral pentadentate n-donor ligand n-methyl-n,n′,n′-tris(2- pyridylmethyl)ethane-1,2-diamine
    • K.D. Koehntop, J.U. Rohde, M. Costas, and L. Que XAS characterization of end-on and side-on peroxoiron(III) complexes of the neutral pentadentate n-donor ligand n-methyl-n,n′,n′-tris(2-pyridylmethyl)ethane-1,2-diamine Dalton Trans. 2004 3191 3198
    • (2004) Dalton Trans. , pp. 3191-3198
    • Koehntop, K.D.1    Rohde, J.U.2    Costas, M.3    Que, L.4
  • 99
    • 41149088130 scopus 로고    scopus 로고
    • Mixed valent sites in biological electron transfer
    • E.I. Solomon, X.J. Xie, and A. Dey Mixed valent sites in biological electron transfer Chem. Soc. Rev. 37 2008 623 638
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 623-638
    • Solomon, E.I.1    Xie, X.J.2    Dey, A.3
  • 101
    • 77954640213 scopus 로고    scopus 로고
    • Probing valence orbital composition with iron K beta X-ray emission spectroscopy
    • N. Lee, T. Petrenko, U. Bergmann, F. Neese, and S. DeBeer Probing valence orbital composition with iron K beta X-ray emission spectroscopy J. Am. Chem. Soc. 132 2010 9715 9727
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9715-9727
    • Lee, N.1    Petrenko, T.2    Bergmann, U.3    Neese, F.4    Debeer, S.5
  • 102
    • 11144306352 scopus 로고    scopus 로고
    • High resolution 1s core hole X-ray spectroscopy in 3d transition metal complexes - Electronic and structural information
    • DOI 10.1016/j.ccr.2004.04.011, PII S0010854504001146, Synchroton Radiation in Inorganic and Bioonorganic Chemistry
    • P. Glatzel, and U. Bergmann High resolution 1s core hole X-ray spectroscopy in 3d transition metal complexes-electronic and structural information Coord. Chem. Rev. 249 2005 65 95 (Pubitemid 40023313)
    • (2005) Coordination Chemistry Reviews , vol.249 , Issue.1-2 , pp. 65-95
    • Glatzel, P.1    Bergmann, U.2
  • 103
    • 0037124234 scopus 로고    scopus 로고
    • Site-selective EXAFS in mixed-valence compounds using high-resolution fluorescence detection: A study of iron in Prussian blue
    • P. Glatzel, L. Jacquamet, U. Bergmann, F.M.F. de Groot, and S.P. Cramer Site-selective EXAFS in mixed-valence compounds using high-resolution fluorescence detection: a study of iron in Prussian blue Inorg. Chem. 41 2002 3121 3127
    • (2002) Inorg. Chem. , vol.41 , pp. 3121-3127
    • Glatzel, P.1    Jacquamet, L.2    Bergmann, U.3    De Groot, F.M.F.4    Cramer, S.P.5
  • 105
    • 0034825092 scopus 로고    scopus 로고
    • Metal Kβ X-ray emission spectra of first row transition metal compounds
    • DOI 10.1016/S0368-2048(00)00416-3
    • S.D. Gamblin, and D.S. Urch Metal K beta X-ray emission spectra of first row transition metal compounds J. Electron Spectr. Relat. Phenom. 113 2001 179 192 (Pubitemid 32874339)
    • (2001) Journal of Electron Spectroscopy and Related Phenomena , vol.113 , Issue.2-3 , pp. 179-192
    • Gamblin, S.D.1    Urch, D.S.2
  • 106
    • 73449130507 scopus 로고    scopus 로고
    • Towards a comprehensive X-ray approach for studying the photosynthetic manganese complex-XANES, K-alpha/K-beta/K-beta-satellite emission lines, RIXS, and comparative computational approaches for selected model complexes
    • 012142
    • I. Zaharieva, P. Chernev, M. Risch, L. Gerencser, G. Berggren, G. Shevchenko, M. Anderlund, T.-C. Weng, M. Haumann, and H. Dau Towards a comprehensive X-ray approach for studying the photosynthetic manganese complex-XANES, K-alpha/K-beta/K-beta-satellite emission lines, RIXS, and comparative computational approaches for selected model complexes J. Phys. Conf. Ser. 190 2009 012142
    • (2009) J. Phys. Conf. Ser. , vol.190
    • Zaharieva, I.1    Chernev, P.2    Risch, M.3    Gerencser, L.4    Berggren, G.5    Shevchenko, G.6    Anderlund, M.7    Weng, T.-C.8    Haumann, M.9    Dau, H.10
  • 108
    • 20444495397 scopus 로고    scopus 로고
    • Energetics of primary and secondary electron transfer in Photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements
    • DOI 10.1016/j.bbabio.2005.03.007, PII S0005272805000897
    • M. Grabolle, and H. Dau Energetics of primary and secondary electron transfer in photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements Biochim. Biophys. Acta 1708 2005 209 218 (Pubitemid 40824951)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1708 , Issue.2 , pp. 209-218
    • Grabolle, M.1    Dau, H.2
  • 109
    • 0026096798 scopus 로고
    • PH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials
    • I. Vass, and S. Styring pH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials Biochemistry 30 1991 830 839
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 110
    • 77955504659 scopus 로고    scopus 로고
    • Density functional theory analysis of structure, energetics, and spectroscopy for the Mn-Fe active site of Chlamydia trachomatis ribonucleotide reductase in four oxidation states
    • W.G. Han, D.A. Giammona, D. Bashford, and L. Noodleman Density functional theory analysis of structure, energetics, and spectroscopy for the Mn-Fe active site of Chlamydia trachomatis ribonucleotide reductase in four oxidation states Inorg. Chem. 49 2010 7266 7281
    • (2010) Inorg. Chem. , vol.49 , pp. 7266-7281
    • Han, W.G.1    Giammona, D.A.2    Bashford, D.3    Noodleman, L.4
  • 111
    • 68149112496 scopus 로고    scopus 로고
    • DFT calculations of comparative energetics and ENDOR/Mössbauer properties for two protonation states of the iron dimer cluster of ribonucleotide reductase intermediate X
    • W.G. Han, and L. Noodleman DFT calculations of comparative energetics and ENDOR/Mössbauer properties for two protonation states of the iron dimer cluster of ribonucleotide reductase intermediate X Dalton Trans. 2009 6045 6057
    • (2009) Dalton Trans. , pp. 6045-6057
    • Han, W.G.1    Noodleman, L.2
  • 112
    • 0033538303 scopus 로고    scopus 로고
    • 2 diamond core. Implications for the core structures of methane monooxygenase intermediate Q and ribonucleotide reductase intermediate X
    • 2 diamond core. Implications for the core structures of methane monooxygenase intermediate Q and ribonucleotide reductase intermediate X J. Am. Chem. Soc. 121 1999 5230 5237
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5230-5237
    • Hsu, H.F.1    Dong, Y.H.2    Shu, L.J.3    Young, V.G.4    Que, L.5
  • 113
    • 0035800409 scopus 로고    scopus 로고
    • Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: A tale of two irons and three proteins
    • DOI 10.1002/1521-3773(20010803)40:15<2782::AID-ANIE2782>3.0.CO;2-P
    • M. Merkx, D.A. Kopp, M.H. Sazinsky, J.L. Blazyk, J. Muller, and S.J. Lippard Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins Angew. Chem. Int. Ed Engl. 40 2001 2782 2807 (Pubitemid 32783348)
    • (2001) Angewandte Chemie - International Edition , vol.40 , Issue.15 , pp. 2782-2807
    • Merkx, M.1    Kopp, D.A.2    Sazinsky, M.H.3    Blazyk, J.L.4    Muandller, J.5    Lippard, S.J.6
  • 114
  • 115
    • 77958609851 scopus 로고    scopus 로고
    • Identification of protonated oxygenic ligands of ribonucleotide reductase intermediate X
    • M. Shanmugam, P.E. Doan, N.S. Lees, J. Stubbe, and B.M. Hoffman Identification of protonated oxygenic ligands of ribonucleotide reductase intermediate X J. Am. Chem. Soc. 131 2009 3370 3376
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3370-3376
    • Shanmugam, M.1    Doan, P.E.2    Lees, N.S.3    Stubbe, J.4    Hoffman, B.M.5
  • 116
    • 33847058857 scopus 로고    scopus 로고
    • (mu-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse
    • D. Yun, R. Garcia-Serres, B.M. Chicalese, Y.H. An, B.H. Huynh, and J.M. Bollinger (mu-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse Biochemistry 46 2007 1925 1932
    • (2007) Biochemistry , vol.46 , pp. 1925-1932
    • Yun, D.1    Garcia-Serres, R.2    Chicalese, B.M.3    An, Y.H.4    Huynh, B.H.5    Bollinger, J.M.6
  • 117
    • 27844488367 scopus 로고    scopus 로고
    • Active site structure of class I ribonucleotide reductase intermediate X: A density functional theory analysis of structure, energetics, and spectroscopy
    • DOI 10.1021/ja050904q
    • W.G. Han, T. Liu, T. Lovell, and L. Noodleman Active site structure of class I ribonucleotide reductase intermediate X: a density functional theory analysis of structure, energetics, and spectroscopy J. Am. Chem. Soc. 127 2005 15778 15790 (Pubitemid 41643288)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.45 , pp. 15778-15790
    • Han, W.-G.1    Liu, T.2    Lovell, T.3    Noodleman, L.4
  • 119
    • 34250811950 scopus 로고    scopus 로고
    • The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state
    • DOI 10.1021/ja072528a
    • W. Jiang, J.M. Bollinger Jr., and C. Krebs The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state J. Am. Chem. Soc. 129 2007 7504 7505 (Pubitemid 46981908)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.24 , pp. 7504-7505
    • Jiang, W.1    Bollinger Jr., J.M.2    Krebs, C.3
  • 120
    • 79955766247 scopus 로고    scopus 로고
    • Oxygen cleavage with manganese and iron in ribonucleotide reductase from Chlamydia trachomatis
    • K. Roos, and P.E. Siegbahn Oxygen cleavage with manganese and iron in ribonucleotide reductase from Chlamydia trachomatis J. Biol. Inorg. Chem. 16 2011 553 565
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 553-565
    • Roos, K.1    Siegbahn, P.E.2
  • 121
    • 0034841065 scopus 로고    scopus 로고
    • 2 activation and radical generation
    • DOI 10.1007/s007750000205
    • M. Högbom, M.E. Andersson, and P. Nordlund Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O-2 activation and radical generation J. Biol. Inorg. Chem. 6 2001 315 323 (Pubitemid 32823963)
    • (2001) Journal of Biological Inorganic Chemistry , vol.6 , Issue.3 , pp. 315-323
    • Hogbom, M.1    Andersson, M.E.2    Nordlund, P.3
  • 123
    • 77955574577 scopus 로고    scopus 로고
    • A tyrosyl-dimanganese coupled spin system is the native metalloradical cofactor of the R2f subunit of the ribonucleotide reductase of Corynebacterium ammoniagenes
    • N. Cox, H. Ogata, P. Stolle, E. Reijerse, G. Auling, and W. Lubitz A tyrosyl-dimanganese coupled spin system is the native metalloradical cofactor of the R2f subunit of the ribonucleotide reductase of Corynebacterium ammoniagenes J. Am. Chem. Soc. 132 2010 11197 11213
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11197-11213
    • Cox, N.1    Ogata, H.2    Stolle, P.3    Reijerse, E.4    Auling, G.5    Lubitz, W.6
  • 124
    • 77956653207 scopus 로고    scopus 로고
    • Structural basis for activation of class Ib ribonucleotide reductase
    • A.K. Boal, J.A. Cotruvo, J. Stubbe, and A.C. Rosenzweig Structural basis for activation of class Ib ribonucleotide reductase Science 329 2010 1526 1530
    • (2010) Science , vol.329 , pp. 1526-1530
    • Boal, A.K.1    Cotruvo, J.A.2    Stubbe, J.3    Rosenzweig, A.C.4
  • 125
    • 0032568594 scopus 로고    scopus 로고
    • Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin
    • X.D. Wang, and L. Que Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin Biochemistry 37 1998 7813 7821
    • (1998) Biochemistry , vol.37 , pp. 7813-7821
    • Wang, X.D.1    Que, L.2
  • 127
    • 58849139303 scopus 로고    scopus 로고
    • Formation and function of the manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase
    • W. Jiang, D. Yun, L. Saleh, J.M. Bollinger Jr., and C. Krebs Formation and function of the manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase Biochemistry 47 2008 13736 13744
    • (2008) Biochemistry , vol.47 , pp. 13736-13744
    • Jiang, W.1    Yun, D.2    Saleh, L.3    Bollinger, Jr.J.M.4    Krebs, C.5
  • 129
    • 2342492837 scopus 로고    scopus 로고
    • Light-induced multistep oxidation of dinuclear manganese complexes for artificial photosynthesis
    • DOI 10.1016/j.jinorgbio.2003.12.009, PII S0162013403004598
    • P. Huang, J. Högblom, M.F. Anderlund, L. Sun, A. Magnuson, and S. Styring Light-induced multistep oxidation of dinuclear manganese complexes for artificial photosynthesis J. Inorg. Biochem. 98 2004 733 745 (Pubitemid 38595276)
    • (2004) Journal of Inorganic Biochemistry , vol.98 , Issue.5 , pp. 733-745
    • Huang, P.1    Hogblom, J.2    Anderlund, M.F.3    Sun, L.4    Magnuson, A.5    Styring, S.6
  • 130
    • 33744509523 scopus 로고    scopus 로고
    • Bridging-type changes facilitate successive oxidation steps at about 1 V in two binuclear manganese complexes-implications for photosynthetic water-oxidation
    • DOI 10.1016/j.jinorgbio.2006.02.001, PII S0162013406000584
    • A. Magnuson, P. Liebisch, J. Högblom, M.F. Anderlund, R. Lomoth, W. Meyer-Klaucke, M. Haumann, and H. Dau Bridging-type changes facilitate successive oxidation steps at about 1 V in two binuclear manganese complexes-implications for photosynthetic water oxidation J. Inorg. Biochem. 100 2006 1234 1243 (Pubitemid 43818123)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.7 , pp. 1234-1243
    • Magnuson, A.1    Liebisch, P.2    Hogblom, J.3    Anderlund, M.F.4    Lomoth, R.5    Meyer-Klaucke, W.6    Haumann, M.7    Dau, H.8


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