메뉴 건너뛰기




Volumn 1844, Issue 3, 2014, Pages 615-622

The ferrous-dioxy complex of Leishmania major globin coupled heme containing adenylate cyclase: The role of proximal histidine on its stability

Author keywords

Adenylate cyclase; Heme protein; Leishmania; O2 sensor; Rapid kinetics and mutation; Steady state catalysis

Indexed keywords

ADENYLATE CYCLASE; APOPROTEIN; CYCLIC AMP; HEME; HEMOPROTEIN; HISTIDINE; IRON; MUTANT PROTEIN; OXYGEN;

EID: 84893367075     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.01.004     Document Type: Article
Times cited : (10)

References (45)
  • 4
    • 0021314377 scopus 로고
    • Bacillus anthracis calmodulin-dependent adenylate cyclase: Chemical and enzymatic properties and interactions with eucaryotic cells
    • S.H. Leppla Bacillus anthracis calmodulin-dependent adenylate cyclase: chemical and enzymatic properties and interactions with eucaryotic cells Adv. Cyclic Nucleotide Protein Phosphorylation Res. 17 1984 189 198
    • (1984) Adv. Cyclic Nucleotide Protein Phosphorylation Res. , vol.17 , pp. 189-198
    • Leppla, S.H.1
  • 5
    • 84885779633 scopus 로고    scopus 로고
    • Globin-coupled heme containing oxygen sensor soluble adenylate cyclase in Leishmania prevents cell death during hypoxia
    • S. Sen Santara, J. Roy, S. Mukherjee, M. Bose, R. Saha, and S. Adak Globin-coupled heme containing oxygen sensor soluble adenylate cyclase in Leishmania prevents cell death during hypoxia Proc. Natl. Acad. Sci. U. S. A. 110 2013 16790 16795
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 16790-16795
    • Sen Santara, S.1    Roy, J.2    Mukherjee, S.3    Bose, M.4    Saha, R.5    Adak, S.6
  • 6
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • M.A. Gilles-Gonzalez, G.S. Ditta, and D.R. Helinski A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti Nature 350 1991 170 172 (Pubitemid 21912192)
    • (1991) Nature , vol.350 , Issue.6314 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 9
    • 33344477903 scopus 로고    scopus 로고
    • Structure-function relationships of EcDOS, a heme-regulated phosphodiesterase from Escherichia coli
    • Y. Sasakura, T. Yoshimura-Suzuki, H. Kurokawa, and T. Shimizu Structure-function relationships of EcDOS, a heme-regulated phosphodiesterase from Escherichia coli Acc. Chem. Res. 39 2006 37 43
    • (2006) Acc. Chem. Res. , vol.39 , pp. 37-43
    • Sasakura, Y.1    Yoshimura-Suzuki, T.2    Kurokawa, H.3    Shimizu, T.4
  • 12
  • 15
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox
    • DOI 10.1016/S0968-0004(97)01110-9, PII S0968000497011109
    • I.B. Zhulin, B.L. Taylor, and R. Dixon PAS domain S-boxes in Archaea, bacteria and sensors for oxygen and redox Trends Biochem. Sci. 22 1997 331 333 (Pubitemid 27376266)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.9 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 16
    • 0035313335 scopus 로고    scopus 로고
    • Recent advances in heme-protein sensors
    • DOI 10.1016/S1367-5931(00)00193-9
    • M.K. Chan Recent advances in heme-protein sensors Curr. Opin. Chem. Biol. 5 2001 216 222 (Pubitemid 32248721)
    • (2001) Current Opinion in Chemical Biology , vol.5 , Issue.2 , pp. 216-222
    • Chan, M.K.1
  • 17
    • 84884781778 scopus 로고    scopus 로고
    • Heme-based globin-coupled oxygen sensors: Linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis
    • M. Martinkova, K. Kitanishi, and T. Shimizu Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis J. Biol. Chem. 288 2013 27702 27711
    • (2013) J. Biol. Chem. , vol.288 , pp. 27702-27711
    • Martinkova, M.1    Kitanishi, K.2    Shimizu, T.3
  • 18
    • 80053896156 scopus 로고    scopus 로고
    • Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5
    • K. Kitanishi, K. Kobayashi, T. Uchida, K. Ishimori, J. Igarashi, and T. Shimizu Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5 J. Biol. Chem. 286 2011 35522 35534
    • (2011) J. Biol. Chem. , vol.286 , pp. 35522-35534
    • Kitanishi, K.1    Kobayashi, K.2    Uchida, T.3    Ishimori, K.4    Igarashi, J.5    Shimizu, T.6
  • 20
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • A. Moglich, R.A. Ayers, and K. Moffat Structure and signaling mechanism of Per-ARNT-Sim domains Structure 17 2009 1282 1294
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Moglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 21
    • 79551613290 scopus 로고    scopus 로고
    • Toward the estimation of the absolute quality of individual protein structure models
    • P. Benkert, M. Biasini, and T. Schwede Toward the estimation of the absolute quality of individual protein structure models Bioinformatics 27 2011 343 350
    • (2011) Bioinformatics , vol.27 , pp. 343-350
    • Benkert, P.1    Biasini, M.2    Schwede, T.3
  • 22
    • 0036783413 scopus 로고    scopus 로고
    • Crystal structures of unligated and CN-ligated Glycera dibranchiata monomer ferric hemoglobin components III and IV
    • DOI 10.1002/prot.10199
    • H.J. Park, C. Yang, N. Treff, J.D. Satterlee, and C. Kang Crystal structures of unligated and CN-ligated Glycera dibranchiata monomer ferric hemoglobin components III and IV Proteins 49 2002 49 60 (Pubitemid 34983173)
    • (2002) Proteins: Structure, Function and Genetics , vol.49 , Issue.1 , pp. 49-60
    • Park, H.-J.1    Yang, C.2    Treff, N.3    Satterlee, J.D.4    Kang, C.5
  • 23
    • 0034716177 scopus 로고    scopus 로고
    • The H93G myoglobin cavity mutant as a versatile template for modeling heme proteins: Ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity
    • DOI 10.1021/ic0007198
    • A.E. Pond, M.P. Roach, M.R. Thomas, S.G. Boxer, and J.H. Dawson The H93G myoglobin cavity mutant as a versatile template for modeling heme proteins: ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity Inorg. Chem. 39 2000 6061 6066 (Pubitemid 32061744)
    • (2000) Inorganic Chemistry , vol.39 , Issue.26 , pp. 6061-6066
    • Pond, A.E.1    Roach, M.P.2    Thomas, M.R.3    Boxer, S.G.4    Dawson, J.H.5
  • 24
    • 0028339218 scopus 로고
    • Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93→Gly
    • DOI 10.1021/bi00187a023
    • D. Barrick Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93→Gly Biochemistry 33 1994 6546 6554 (Pubitemid 24189368)
    • (1994) Biochemistry , vol.33 , Issue.21 , pp. 6546-6554
    • Barrick, D.1
  • 25
    • 0029918810 scopus 로고    scopus 로고
    • Trans effects in nitric oxide binding to myoglobin cavity mutant H93G
    • DOI 10.1021/bi951661p
    • S.M. Decatur, S. Franzen, G.D. DePillis, R.B. Dyer, W.H. Woodruff, and S.G. Boxer Trans effects in nitric oxide binding to myoglobin cavity mutant H93G Biochemistry 35 1996 4939 4944 (Pubitemid 26126710)
    • (1996) Biochemistry , vol.35 , Issue.15 , pp. 4939-4944
    • Decatur, S.M.1    Franzen, S.2    DePillis, G.D.3    Dyer, R.B.4    Woodruff, W.H.5    Boxer, S.G.6
  • 26
    • 84873038246 scopus 로고    scopus 로고
    • Mutation of Val90 to His in the pseudoperoxidase from Leishmania major enhances peroxidase activity
    • R. Saha, M. Bose, and S. Adak Mutation of Val90 to His in the pseudoperoxidase from Leishmania major enhances peroxidase activity Biochim. Biophys. Acta 1834 2013 651 657
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 651-657
    • Saha, R.1    Bose, M.2    Adak, S.3
  • 27
    • 41949126490 scopus 로고    scopus 로고
    • Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major-kinetic studies on Trp208Phe mutant and wild type enzyme
    • R.K. Yadav, S. Dolai, S. Pal, and S. Adak Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major-kinetic studies on Trp208Phe mutant and wild type enzyme Biochim. Biophys. Acta 1784 2008 863 871
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 863-871
    • Yadav, R.K.1    Dolai, S.2    Pal, S.3    Adak, S.4
  • 28
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen)
    • K.G. Paul, H. Theorell, and A. Akeson The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen) Acta Chem. Scand. 7 1953 1284 1287
    • (1953) Acta Chem. Scand. , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 31
    • 0030811194 scopus 로고    scopus 로고
    • Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands
    • DOI 10.1074/jbc.272.27.16746
    • S.M. Duff, J.B. Wittenberg, and R.D. Hill Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands J. Biol. Chem. 272 1997 16746 16752 (Pubitemid 27289769)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.27 , pp. 16746-16752
    • Duff, S.M.G.1    Wittenberg, J.B.2    Hill, R.D.3
  • 33
    • 84884164092 scopus 로고    scopus 로고
    • The heme-based oxygen-sensor phosphodiesterase Ec DOS (DosP): Structure-function relationships
    • T. Shimizu The heme-based oxygen-sensor phosphodiesterase Ec DOS (DosP): structure-function relationships Biosensors 3 2013 211 237
    • (2013) Biosensors , vol.3 , pp. 211-237
    • Shimizu, T.1
  • 34
    • 0000754869 scopus 로고
    • The absorption spectra of hemoglobin and its derivatives in the visible and near infra-red regions
    • B.L. Horecker The absorption spectra of hemoglobin and its derivatives in the visible and near infra-red regions J. Biol. Chem. 148 1943 173 183
    • (1943) J. Biol. Chem. , vol.148 , pp. 173-183
    • Horecker, B.L.1
  • 35
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen
    • J.T. Trent III, R.A. Watts, and M.S. Hargrove Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen J. Biol. Chem. 276 2001 30106 30110
    • (2001) J. Biol. Chem. , vol.276 , pp. 30106-30110
    • Trent III, J.T.1    Watts, R.A.2    Hargrove, M.S.3
  • 36
    • 7244245630 scopus 로고    scopus 로고
    • Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin: Molecular mechanisms and physiological significance
    • DOI 10.1074/jbc.M407126200
    • A. Fago, C. Hundahl, S. Dewilde, K. Gilany, L. Moens, and R.E. Weber Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin, molecular mechanisms and physiological significance J. Biol. Chem. 279 2004 44417 44426 (Pubitemid 39430847)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44417-44426
    • Fago, A.1    Hundahl, C.2    Dewilde, S.3    Gilany, K.4    Moens, L.5    Weber, R.E.6
  • 37
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • DOI 10.1021/bi00192a011
    • M.A. Gilles-Gonzalez, G. Gonzalez, M.F. Perutz, L. Kiger, M.C. Marden, and C. Poyart Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation Biochemistry 33 1994 8067 8073 (Pubitemid 24223828)
    • (1994) Biochemistry , vol.33 , Issue.26 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 38
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • DOI 10.1021/bi991911s
    • V.M. Delgado-Nixon, G. Gonzalez, and M.A. Gilles-Gonzalez Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor Biochemistry 39 2000 2685 2691 (Pubitemid 30148922)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.-A.3
  • 39
    • 0027368854 scopus 로고
    • High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
    • DOI 10.1006/jmbi.1993.1569
    • M.L. Quillin, R.M. Arduini, J.S. Olson, and G.N. Phillips Jr. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin J. Mol. Biol. 234 1993 140 155 (Pubitemid 23337970)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.1 , pp. 140-155
    • Quillin, M.L.1    Arduini, R.M.2    Olson, J.S.3    Phillips Jr., G.N.4
  • 40
    • 0017349738 scopus 로고
    • Structure of myoglobin refined at 2.O Å resolution. II. Structure of deoxymyoglobin from sperm whale
    • T. Takano Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale J. Mol. Biol. 110 1977 569 584 (Pubitemid 8050925)
    • (1977) Journal of Molecular Biology , vol.110 , Issue.3 , pp. 569-584
    • Takano, T.1
  • 41
    • 57649114078 scopus 로고    scopus 로고
    • Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: Roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding
    • A. Tanaka, and T. Shimizu Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding Biochemistry 47 2008 13438 13446
    • (2008) Biochemistry , vol.47 , pp. 13438-13446
    • Tanaka, A.1    Shimizu, T.2
  • 42
    • 0037195260 scopus 로고    scopus 로고
    • 2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum
    • DOI 10.1021/bi020144l
    • 2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum Biochemistry 41 2002 12952 12958 (Pubitemid 35215778)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12952-12958
    • Hao, B.1    Isaza, C.2    Arndt, J.3    Soltis, M.4    Chan, M.K.5
  • 44
    • 0346732270 scopus 로고    scopus 로고
    • Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion and site-directed mutants
    • DOI 10.1074/jbc.M304408200
    • T. Yoshimura, I. Sagami, Y. Sasakura, and T. Shimizu Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a study of deletion and site-directed mutants J. Biol. Chem. 278 2003 53105 53111 (Pubitemid 38035914)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 53105-53111
    • Yoshimura, T.1    Sagami, I.2    Sasakura, Y.3    Shimizu, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.