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Volumn 106, Issue 52, 2009, Pages 22090-22095

Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation

Author keywords

Cytochrome c oxidase; H2S complex; Reversible inhibition; Synthetic functional model

Indexed keywords

COPPER; CYTOCHROME C OXIDASE; HEME; HYDROGEN SULFIDE; IRON; OXYGEN; PORPHYRIN DERIVATIVE;

EID: 76049087222     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0904082106     Document Type: Article
Times cited : (134)

References (39)
  • 1
    • 0016395477 scopus 로고
    • A paramagnetic dioxygen complex of iron II derived from a picket fence porphyrin further models for hemoproteins
    • Collman JP, Gagne RR, Reed CA (1974) A paramagnetic dioxygen complex of iron II derived from a picket fence porphyrin further models for hemoproteins. J Am Chem Soc 96:2629-2631.
    • (1974) J Am Chem Soc , vol.96 , pp. 2629-2631
    • Collman, J.P.1    Gagne, R.R.2    Reed, C.A.3
  • 2
    • 0015923308 scopus 로고
    • Reversible oxygen adduct formation in ferrous complexes derived from a picket fence porphyrin model for oxy myoglobin
    • Collman JP, Gagne RR, Halbert TR, Marchon JC, Reed CA (1973) Reversible oxygen adduct formation in ferrous complexes derived from a picket fence porphyrin model for oxy myoglobin. J Am Chem Soc 95:7868-7870.
    • (1973) J Am Chem Soc , vol.95 , pp. 7868-7870
    • Collman, J.P.1    Gagne, R.R.2    Halbert, T.R.3    Marchon, J.C.4    Reed, C.A.5
  • 4
    • 0016856701 scopus 로고
    • Picket-Fence Porphyrins. Synthetic Models for Oxygen Binding Hemoproteins
    • Collman JP, et al. (1975) Picket-Fence Porphyrins. Synthetic Models for Oxygen Binding Hemoproteins. J Am Chem Soc 97:1427-1439.
    • (1975) J Am Chem Soc , vol.97 , pp. 1427-1439
    • Collman, J.P.1
  • 6
    • 1542334754 scopus 로고    scopus 로고
    • Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin
    • Collman JP, Boulatov R, Sunderland CJ, Fu L (2004) Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin. Chem Rev 104:561-588.
    • (2004) Chem Rev , vol.104 , pp. 561-588
    • Collman, J.P.1    Boulatov, R.2    Sunderland, C.J.3    Fu, L.4
  • 7
    • 0032837780 scopus 로고    scopus 로고
    • Synthetic models for hemoglobin and myoglobin
    • Collman JP, Fu L (1999) Synthetic models for hemoglobin and myoglobin. Acc Chem Res 32:455-463.
    • (1999) Acc Chem Res , vol.32 , pp. 455-463
    • Collman, J.P.1    Fu, L.2
  • 8
    • 0001277126 scopus 로고    scopus 로고
    • Dioxygen and carbon monoxide binding in dendritic iron(II)porphyrins
    • Collman JP, Fu L, Zingg A, Diederich F (1997) Dioxygen and carbon monoxide binding in dendritic iron(II)porphyrins. Chem Comm 2:193-194.
    • (1997) Chem Comm , vol.2 , pp. 193-194
    • Collman, J.P.1    Fu, L.2    Zingg, A.3    Diederich, F.4
  • 9
    • 33947379088 scopus 로고    scopus 로고
    • A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux
    • Collman JP, et al. (2007) A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux. Science 315:1565-1568.
    • (2007) Science , vol.315 , pp. 1565-1568
    • Collman, J.P.1
  • 10
    • 48249093022 scopus 로고    scopus 로고
    • Interaction of nitric oxide with a functional model of cytochrome c oxidase
    • Collman JP, et al. (2008) Interaction of nitric oxide with a functional model of cytochrome c oxidase. Proc Natl Acad Sci USA 105:9892-9896.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9892-9896
    • Collman, J.P.1
  • 11
    • 57449091270 scopus 로고    scopus 로고
    • Antagonism of Nitric Oxide Toward the Inhibition of Cytochrome c Oxidase by Carbon Monoxide and Cyanide
    • Pearce LL, Manzano EL, Martinez-Bosch S, Peterson J (2008) Antagonism of Nitric Oxide Toward the Inhibition of Cytochrome c Oxidase by Carbon Monoxide and Cyanide Chem Res Toxicol 21:2073-2081.
    • (2008) Chem Res Toxicol , vol.21 , pp. 2073-2081
    • Pearce, L.L.1    Manzano, E.L.2    Martinez-Bosch, S.3    Peterson, J.4
  • 13
    • 0036146130 scopus 로고    scopus 로고
    • Cytochrome oxidase inhibition induced by acute hydrogen sulfide inhalation: Correlation with tissue sulfide concentrations in the rat brain, liver, lung, and nasal epithelium
    • Dorman DC, et al. (2002) Cytochrome oxidase inhibition induced by acute hydrogen sulfide inhalation: Correlation with tissue sulfide concentrations in the rat brain, liver, lung, and nasal epithelium Toxicol Sci 65:18-25.
    • (2002) Toxicol Sci , vol.65 , pp. 18-25
    • Dorman, D.C.1
  • 14
    • 0025218713 scopus 로고
    • Effects of hydrogen-sulfide exposure on lung mitochondrial respiratory-chain enzymes in rats
    • Khan AA, et al. (1990) Effects of hydrogen-sulfide exposure on lung mitochondrial respiratory-chain enzymes in rats. Toxicol Appl Pharmacol 103:482-490.
    • (1990) Toxicol Appl Pharmacol , vol.103 , pp. 482-490
    • Khan, A.A.1
  • 15
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabo C (2007) Hydrogen sulphide and its therapeutic potential. Nat Rev Drug Discovery 6:917-935.
    • (2007) Nat Rev Drug Discovery , vol.6 , pp. 917-935
    • Szabo, C.1
  • 16
    • 0036845556 scopus 로고    scopus 로고
    • Two's company, three's a crowd: Can H2S be the third endogenous gaseous transmitter?
    • Wang R (2002) Two's company, three's a crowd: Can H2S be the third endogenous gaseous transmitter? FASEB J 16:1792-1798.
    • (2002) FASEB J , vol.16 , pp. 1792-1798
    • Wang, R.1
  • 17
    • 34047142764 scopus 로고    scopus 로고
    • Hydrogen sulfide (H2S) - the third gas for interest for pharmacologists
    • 59:4-24
    • Lowicka E, Beltowski J (2007) Hydrogen sulfide (H2S) - the third gas for interest for pharmacologists. Pharmalogical Reports 59:4-24.
    • (2007) Pharmalogical Reports
    • Lowicka, E.1    Beltowski, J.2
  • 18
    • 41149146946 scopus 로고    scopus 로고
    • Inhaled hydrogen sufide - A rapidly reversible inhibitor of cardiac and metabolic function in the mouse
    • Volpato GP, et al. (2008) Inhaled hydrogen sufide - A rapidly reversible inhibitor of cardiac and metabolic function in the mouse. Anestaesiology 108:659-668.
    • (2008) Anestaesiology , vol.108 , pp. 659-668
    • Volpato, G.P.1
  • 19
    • 39649106917 scopus 로고    scopus 로고
    • Is human hibernation possible?
    • Lee CC (2008) Is human hibernation possible? Annu Rev Med 59:177-186.
    • (2008) Annu Rev Med , vol.59 , pp. 177-186
    • Lee, C.C.1
  • 20
    • 20244390001 scopus 로고    scopus 로고
    • H2S induces a suspended animation-like state in mice
    • Blackstone E, Morrison M, Roth MB (2005) H2S induces a suspended animation-like state in mice. Science 308:518.
    • (2005) Science , vol.308 , pp. 518
    • Blackstone, E.1    Morrison, M.2    Roth, M.B.3
  • 21
    • 3543017385 scopus 로고    scopus 로고
    • Natural hypometabolism during hibernation and daily torpor in mammals
    • Heldmaier G, Ortmann S, Elvert R (2004) Natural hypometabolism during hibernation and daily torpor in mammals. Respir Physiol Neurobiol 141:317-329.
    • (2004) Respir Physiol Neurobiol , vol.141 , pp. 317-329
    • Heldmaier, G.1    Ortmann, S.2    Elvert, R.3
  • 22
    • 34247093873 scopus 로고    scopus 로고
    • Suspended animation-like state protects mice from lethal hypoxia
    • Blackstone E, Roth MB (2007) Suspended animation-like state protects mice from lethal hypoxia. Shock 27:370-372.
    • (2007) Shock , vol.27 , pp. 370-372
    • Blackstone, E.1    Roth, M.B.2
  • 23
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance
    • Cooper CE, Brown GC (2008) The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance. J Bionenerg Biomembr 40:533-539.
    • (2008) J Bionenerg Biomembr , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 24
    • 0017353388 scopus 로고
    • The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase
    • Petersen LC (1977) The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase. Biochim Biophys Acta 460:299-307.
    • (1977) Biochim Biophys Acta , vol.460 , pp. 299-307
    • Petersen, L.C.1
  • 25
    • 18144447465 scopus 로고    scopus 로고
    • Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase
    • Yoshikawa S, et al. (1998) Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280:1723-1729.
    • (1998) Science , vol.280 , pp. 1723-1729
    • Yoshikawa, S.1
  • 26
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson Miller S, Babcock GT (1996) Heme/copper terminal oxidases. Chem Rev 96:2889-2907.
    • (1996) Chem Rev , vol.96 , pp. 2889-2907
    • Ferguson Miller, S.1    Babcock, G.T.2
  • 27
    • 0028890031 scopus 로고
    • Structure at 2.8A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H (1995) Structure at 2.8A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 28
    • 0035382613 scopus 로고    scopus 로고
    • Cytochrome c oxidase and the regulation of oxidative phosphorylation
    • Ludwig B, et al. (2001) Cytochrome c oxidase and the regulation of oxidative phosphorylation. Chem Bio Chem 2:392-403.
    • (2001) Chem Bio Chem , vol.2 , pp. 392-403
    • Ludwig, B.1
  • 29
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock GT, Wikstrom M (1992) Oxygen activation and the conservation of energy in cell respiration. Nature 356:301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikstrom, M.2
  • 30
    • 2442420933 scopus 로고    scopus 로고
    • Synthesis of cytochrome c oxidase models bearing a Tyr(244) mimic
    • Collman JP, Decreau RA, Zhang C (2004) Synthesis of cytochrome c oxidase models bearing a Tyr(244) mimic. J Org Chem 69:3546-3549.
    • (2004) J Org Chem , vol.69 , pp. 3546-3549
    • Collman, J.P.1    Decreau, R.A.2    Zhang, C.3
  • 31
    • 64849089426 scopus 로고    scopus 로고
    • Catalytic Reduction of O2 by Cytochrome c Using a Synthetic Model of Cytochrome c Oxidase
    • Collman JP, Gosh S, Dey A, Decreau RA, Yang Y (2009) Catalytic Reduction of O2 by Cytochrome c Using a Synthetic Model of Cytochrome c Oxidase. J Am Chem Soc 131:5034-5035.
    • (2009) J Am Chem Soc , vol.131 , pp. 5034-5035
    • Collman, J.P.1    Gosh, S.2    Dey, A.3    Decreau, R.A.4    Yang, Y.5
  • 32
    • 33748217014 scopus 로고
    • Proof of Strong S-H * - S Bridges in [Ru(SH2)(PPh,)('S4')] * THF, the First H2S Complex Characterized by X-Ray Crystallography
    • Sellman D, Lechner P, Knoch F, Moll M (1991) Proof of Strong S-H * - S Bridges in [Ru(SH2)(PPh,)('S4')] * THF, the First H2S Complex Characterized by X-Ray Crystallography. Angew Chem, Int Ed 552-553.
    • (1991) Angew Chem, Int Ed , pp. 552-553
    • Sellman, D.1    Lechner, P.2    Knoch, F.3    Moll, M.4
  • 33
    • 84986734571 scopus 로고
    • Raman and infrared study of the low temperature phase of solid H2S and D2S
    • Anderson A, Binbrekt S, Tang HC (1977) Raman and infrared study of the low temperature phase of solid H2S and D2S. J Raman Spectrosc 6:213-220.
    • (1977) J Raman Spectrosc , vol.6 , pp. 213-220
    • Anderson, A.1    Binbrekt, S.2    Tang, H.C.3
  • 35
    • 33845214073 scopus 로고
    • Ammineruthenium Complexes of Hydrogen Sulfide and Related Sulfur Ligands
    • Kuehn CG, Taube H (1976) Ammineruthenium Complexes of Hydrogen Sulfide and Related Sulfur Ligands. J Am Chem Soc 98:689-702.
    • (1976) J Am Chem Soc , vol.98 , pp. 689-702
    • Kuehn, C.G.1    Taube, H.2
  • 36
    • 34248550962 scopus 로고    scopus 로고
    • Intramolecular singleturnover reaction in a cytochrome c oxidase model bearing a Tyr244 mimic
    • Collman JP, Decreau RA, Yan Y, Yoon J, Solomon EI (2007) Intramolecular singleturnover reaction in a cytochrome c oxidase model bearing a Tyr244 mimic. J Am Chem Soc 129:5794-5795.
    • (2007) J Am Chem Soc , vol.129 , pp. 5794-5795
    • Collman, J.P.1    Decreau, R.A.2    Yan, Y.3    Yoon, J.4    Solomon, E.I.5
  • 37
    • 0038209163 scopus 로고    scopus 로고
    • Spectroscopic evidence for a heme-superoxide/Cu(I) intermediate in a functional model of cytochrome c oxidase
    • Collman JP, Sunderland CJ, Berg KE, Vance MA, Solomon EI (2003) Spectroscopic evidence for a heme-superoxide/Cu(I) intermediate in a functional model of cytochrome c oxidase. J Am Chem Soc 125:6648-6649.
    • (2003) J Am Chem Soc , vol.125 , pp. 6648-6649
    • Collman, J.P.1    Sunderland, C.J.2    Berg, K.E.3    Vance, M.A.4    Solomon, E.I.5
  • 38
    • 0021665682 scopus 로고
    • Low-spin ferric forms of cytochrome-a3 in mixed-ligand and partially reduced cyanide-bound derivatives of cytochrome c oxidase
    • Hill BC, et al. (1984) Low-spin ferric forms of cytochrome-a3 in mixed-ligand and partially reduced cyanide-bound derivatives of cytochrome c oxidase. Biochem J 224:591-600.
    • (1984) Biochem J , vol.224 , pp. 591-600
    • Hill, B.C.1
  • 39
    • 0020149565 scopus 로고
    • Sulfide as an inhibitor and electron-donor for the cytochrome c oxidase system
    • Nicholls P, Kim JK (1982) Sulfide as an inhibitor and electron-donor for the cytochrome c oxidase system. Can J Biochem 60:613-623.
    • (1982) Can J Biochem , vol.60 , pp. 613-623
    • Nicholls, P.1    Kim, J.K.2


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