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Volumn 106, Issue 11, 2009, Pages 4101-4105

Water may inhibit oxygen binding in hemoprotein models

Author keywords

Spin cross over; Tris imidazole pocket; Water cluster

Indexed keywords

CYTOCHROME C OXIDASE; HEMOPROTEIN; IMIDAZOLE; METAL ION; OXYGEN; WATER;

EID: 63149182644     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0900893106     Document Type: Article
Times cited : (36)

References (52)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 63149171914 scopus 로고
    • Regulation of oxygen-affinity of hemoglobin. Influence of structure of the globin on the heme iron
    • Perutz MF (1979) Regulation of oxygen-affinity of hemoglobin. Influence of structure of the globin on the heme iron. Annu Rev Biochem 94:699-714.
    • (1979) Annu Rev Biochem , vol.94 , pp. 699-714
    • Perutz, M.F.1
  • 6
    • 37049049612 scopus 로고
    • Nature of iron-oxygen bond in oxyhaemoglobin
    • Pauling L, Weiss JJ (1964) Nature of iron-oxygen bond in oxyhaemoglobin. Nature 203:182-183.
    • (1964) Nature , vol.203 , pp. 182-183
    • Pauling, L.1    Weiss, J.J.2
  • 7
    • 0037121883 scopus 로고    scopus 로고
    • Distal metal effects in cobalt porphyrins related to CcO
    • Collman JP, et al. (2002) Distal metal effects in cobalt porphyrins related to CcO. Inorg Chem 41:6583-6596.
    • (2002) Inorg Chem , vol.41 , pp. 6583-6596
    • Collman, J.P.1
  • 8
    • 0027368854 scopus 로고
    • High-resolution crystal-structures of distal histidine mutants of sperm whale myoglobin
    • Quillin ML, Arduini RM, Olson JS, Phillips GN (1993) High-resolution crystal-structures of distal histidine mutants of sperm whale myoglobin. J Mol Biol 234:140-155.
    • (1993) J Mol Biol , vol.234 , pp. 140-155
    • Quillin, M.L.1    Arduini, R.M.2    Olson, J.S.3    Phillips, G.N.4
  • 10
    • 1942536646 scopus 로고    scopus 로고
    • Proton-coupled electron transfer: A unifying mechanism for biological charge transport, amino acid radical initiation and propagation, and bond making/breaking reactions of water and oxygen
    • Chang CJ, Chang MCY, Damrauer NH, Nocera DG (2004) Proton-coupled electron transfer: A unifying mechanism for biological charge transport, amino acid radical initiation and propagation, and bond making/breaking reactions of water and oxygen. Biochim Biophys Acta 1655:13-28.
    • (2004) Biochim Biophys Acta , vol.1655 , pp. 13-28
    • Chang, C.J.1    Chang, M.C.Y.2    Damrauer, N.H.3    Nocera, D.G.4
  • 11
    • 34247180567 scopus 로고    scopus 로고
    • The proton pumping pathway of bovine heart cytochrome c oxidase
    • Shimokata K, et al. (2007) The proton pumping pathway of bovine heart cytochrome c oxidase. Proc Natl Acad Sci USA 104:4200-4205.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4200-4205
    • Shimokata, K.1
  • 12
    • 5244280148 scopus 로고    scopus 로고
    • Crystal structure of fully oxidized bovine heart cytochrome c oxidase at 2.8 angstrom resolution: A review
    • Yoshikawa S, Tsukihara T, Shinzawa Itoh K (1996) Crystal structure of fully oxidized bovine heart cytochrome c oxidase at 2.8 angstrom resolution: A review. Biochem Moscow 61:1369-1376.
    • (1996) Biochem Moscow , vol.61 , pp. 1369-1376
    • Yoshikawa, S.1    Tsukihara, T.2    Shinzawa Itoh, K.3
  • 13
    • 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
  • 14
    • 0029652024 scopus 로고
    • Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 A
    • Tsukihara T, et al. (1995) Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 A. Science 269:1069-1074.
    • (1995) Science , vol.269 , pp. 1069-1074
    • Tsukihara, T.1
  • 15
    • 0020749147 scopus 로고
    • O2and CO binding to iron(II) porphyrins. Acomparison of the picket fence and pocket porphyrins
    • Collman JP, et al. (1983) O2and CO binding to iron(II) porphyrins. Acomparison of the picket fence and pocket porphyrins. J Am Chem Soc 105:3052-3064.
    • (1983) J Am Chem Soc , vol.105 , pp. 3052-3064
    • Collman, J.P.1
  • 16
    • 0000795109 scopus 로고
    • Resonance Raman spectra of (dioxygen) (porphyrinato) (hindered imidazole) iron (II) complexes. Implications for hemoglobin cooperativity
    • Walters MA, Spiro TG, Suslick KS, Collman JP (1980) Resonance Raman spectra of (dioxygen) (porphyrinato) (hindered imidazole) iron (II) complexes. Implications for hemoglobin cooperativity. JAm Chem Soc 102:6857-6858.
    • (1980) JAm Chem Soc , vol.102 , pp. 6857-6858
    • Walters, M.A.1    Spiro, T.G.2    Suslick, K.S.3    Collman, J.P.4
  • 17
    • 0025311306 scopus 로고
    • Direct detection of a dioxygen adduct of cytochrome a3 in the mixed-valence cytochrome-oxidase dioxygen reaction
    • Varotsis C, Woodruff WH, Babcock GT(1990) Direct detection of a dioxygen adduct of cytochrome a3 in the mixed-valence cytochrome-oxidase dioxygen reaction. J Biol Chem 265:11131-11136.
    • (1990) J Biol Chem , vol.265 , pp. 11131-11136
    • Varotsis, C.1    Woodruff, W.H.2    Babcock, G.T.3
  • 18
    • 0019330565 scopus 로고
    • Resonance Raman of myoglobin reconstituted with spirographis and iso spirographis hemes and iron 2, 4-diformyl- protoporphyrin IX effect of formyl substitution at the heme periphery
    • Nagai K, Kitagawa T (1980) Resonance Raman of myoglobin reconstituted with spirographis and iso spirographis hemes and iron 2, 4-diformyl- protoporphyrin IX effect of formyl substitution at the heme periphery. Biochemistry19:379-385.
    • (1980) Biochemistry , vol.19 , pp. 379-385
    • Nagai, K.1    Kitagawa, T.2
  • 19
    • 0001572585 scopus 로고
    • Structure-sensitive resonance Raman bandsoftetraphenyl and picket fence porphyrin-iron complexes, including an oxyhemoglobin analog
    • Burke JM, et al. (1978) Structure-sensitive resonance Raman bandsoftetraphenyl and picket fence porphyrin-iron complexes, including an oxyhemoglobin analog. J Am Chem Soc 100:6083-6088.
    • (1978) J Am Chem Soc , vol.100 , pp. 6083-6088
    • Burke, J.M.1
  • 20
    • 0006690931 scopus 로고
    • Spectra and reaction kinetics of respiratory pigments of homogenized and intact cells
    • Chance B (1952) Spectra and reaction kinetics of respiratory pigments of homogenized and intact cells. Nature 169:215-221.
    • (1952) Nature , vol.169 , pp. 215-221
    • Chance, B.1
  • 21
    • 0014216570 scopus 로고
    • Reaction of reduced cytochrome c oxidase with oxygen
    • Greenwood C, Gibson QH (1967) Reaction of reduced cytochrome c oxidase with oxygen. J Biol Chem 242:1782-1787.
    • (1967) J Biol Chem , vol.242 , pp. 1782-1787
    • Greenwood, C.1    Gibson, Q.H.2
  • 23
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energyin cell respiration
    • Babcock GT, Wikstrom M (1992) Oxygen activation and the conservation of energyin cell respiration. Nature 356:301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikstrom, M.2
  • 24
    • 3042907629 scopus 로고
    • Synthetic heme dioxygen complexes
    • Momenteau M, Reed CA (1994) Synthetic heme dioxygen complexes. Chem Rev 94:659-698.
    • (1994) Chem Rev , vol.94 , pp. 659-698
    • Momenteau, M.1    Reed, C.A.2
  • 25
    • 0014028073 scopus 로고
    • Reactions of isolated alpha and beta chains of human hemoglobin with oxygen and carbon monoxide
    • Brunori M, Noble RW,Antonini E, Wyman J (1966)Reactions of isolated alpha and beta chains of human hemoglobin with oxygen and carbon monoxide. J Biol Chem 241:5238-5243.
    • (1966) J Biol Chem , vol.241 , pp. 5238-5243
    • Brunori, M.1    Noble, R.W.2    Antonini, E.3    Wyman, J.4
  • 26
    • 0023723437 scopus 로고
    • The role of the distal histidine in myoglobin and hemoglobin
    • Olson JS, et al. (1988) The role of the distal histidine in myoglobin and hemoglobin. Nature 336:265-266.
    • (1988) Nature , vol.336 , pp. 265-266
    • Olson, J.S.1
  • 27
    • 2442616950 scopus 로고    scopus 로고
    • How O2binds to heme. Reasons for rapid binding and spin inversion
    • Jensen KP, Ryde U(2004) How O2binds to heme. Reasons for rapid binding and spin inversion. JBiol Chem 279:14561-14569.
    • (2004) JBiol Chem , vol.279 , pp. 14561-14569
    • Jensen, K.P.1    Ryde, U.2
  • 29
    • 63149146499 scopus 로고
    • eds Agarwala BV, Munshi KN World Scientific, Singapore, River Edge, pp
    • Basolo F (1993) in Facets of Coordination Chemistry, eds Agarwala BV, Munshi KN (World Scientific, Singapore, River Edge), pp 31-32.
    • (1993) Facets of Coordination Chemistry , pp. 31-32
    • Basolo, F.1
  • 30
    • 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
  • 31
    • 0017049582 scopus 로고
    • Electronic state of heme in cytochrome- oxidase. 1. Magnetic circular dichroism of isolated enzyme and its derivative
    • Babcock GT, Vickery LE, Palmer G (1976) Electronic state of heme in cytochrome- oxidase. 1. Magnetic circular dichroism of isolated enzyme and its derivative. J Biol Chem 251:7907-7919.
    • (1976) J Biol Chem , vol.251 , pp. 7907-7919
    • Babcock, G.T.1    Vickery, L.E.2    Palmer, G.3
  • 32
    • 16944362191 scopus 로고    scopus 로고
    • Aza-crown-capped porphyrin models of myoglobin: Studies of the steric interactions of gas binding
    • Collman JP,et al. (1997)Aza-crown-capped porphyrin models of myoglobin: Studies of the steric interactions of gas binding. J Am Chem Soc 119:3481-3489.
    • (1997) J Am Chem Soc , vol.119 , pp. 3481-3489
    • Collman, J.P.1
  • 33
    • 0037155994 scopus 로고    scopus 로고
    • Biomimetic studies ofterminal oxidases: Trisimidazole picket metalloporphyrins
    • BoulatovR
    • Collman JP, Sunderland CJ, BoulatovR (2002) Biomimetic studies ofterminal oxidases: Trisimidazole picket metalloporphyrins. Inorg Chem 41:2282-2291.
    • (2002) Inorg Chem , vol.41 , pp. 2282-2291
    • Collman, J.P.1    Sunderland, C.J.2
  • 34
    • 0001602005 scopus 로고
    • Synthesis and characterization of tailed picketfence porphyrins
    • Collman JP, et al. (1980) Synthesis and characterization of tailed picketfence porphyrins. JAm Chem Soc 102:4182-4192.
    • (1980) JAm Chem Soc , vol.102 , pp. 4182-4192
    • Collman, J.P.1
  • 35
    • 0000998961 scopus 로고
    • Synthesisand characterization of the pocketporphyrins
    • Collman JP, et al. (1983) Synthesisand characterization of the pocketporphyrins. J Am Chem Soc 105:3038-3052.
    • (1983) J Am Chem Soc , vol.105 , pp. 3038-3052
    • Collman, J.P.1
  • 36
    • 0015931666 scopus 로고
    • Proton nuclear magnetic-resonance and electron-spin resonance investigation of electronic-structure and magnetic properties of synthetic low spin ferric porphyrins
    • Lamar GN, Walker FA (1973) Proton nuclear magnetic-resonance and electron-spin resonance investigation of electronic-structure and magnetic properties of synthetic low spin ferric porphyrins. JAm Chem Soc 95:1782-1790.
    • (1973) JAm Chem Soc , vol.95 , pp. 1782-1790
    • Lamar, G.N.1    Walker, F.A.2
  • 37
    • 0017782878 scopus 로고
    • Nuclear magnetic resonance investigation of magneticand electronic properties of intermediate spin ferrousporphyrin complexes
    • Goff H, Lamar GN, Reed CA (1977) Nuclear magnetic resonance investigation of magneticand electronic properties of intermediate spin ferrousporphyrin complexes. J Am Chem Soc 99:3641-3646.
    • (1977) J Am Chem Soc , vol.99 , pp. 3641-3646
    • Goff, H.1    Lamar, G.N.2    Reed, C.A.3
  • 38
    • 0017785182 scopus 로고
    • High-spin ferrous porphyrin complexes as models for deoxymyoglobin and deoxyhemoglobin. Proton nuclear magnetic-resonance study
    • Goff H, Lamar GN (1977) High-spin ferrous porphyrin complexes as models for deoxymyoglobin and deoxyhemoglobin. Proton nuclear magnetic-resonance study. J Am Chem Soc 99:6599-6606.
    • (1977) J Am Chem Soc , vol.99 , pp. 6599-6606
    • Goff, H.1    Lamar, G.N.2
  • 39
    • 0038615235 scopus 로고
    • Fischer, Karl coulometry. The cathode reaction
    • Scholz E (1994) Fischer, Karl coulometry. The cathode reaction. Fresenius J Anal Chem 348:269-271.
    • (1994) Fresenius J Anal Chem , vol.348 , pp. 269-271
    • Scholz, E.1
  • 41
    • 0035387452 scopus 로고    scopus 로고
    • Studies on the structure of water using two-dimensional near-infrared correlation spectroscopy and principal component analysis
    • Segtan VH, Sasic S, Isaksson T, Ozaki Y (2001) Studies on the structure of water using two-dimensional near-infrared correlation spectroscopy and principal component analysis. Anal Chem 73:3153-3161.
    • (2001) Anal Chem , vol.73 , pp. 3153-3161
    • Segtan, V.H.1    Sasic, S.2    Isaksson, T.3    Ozaki, Y.4
  • 43
    • 0030987236 scopus 로고    scopus 로고
    • Identification of a functional water channel in cytochrome P450 enzymes
    • Oprea TI, Hummer G, Garcia AE (1997) Identification of a functional water channel in cytochrome P450 enzymes. Proc Natl Acad Sci USA94:2133-2138.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2133-2138
    • Oprea, T.I.1    Hummer, G.2    Garcia, A.E.3
  • 44
    • 0032538786 scopus 로고    scopus 로고
    • On the origin of the low-spin character of cytochrome P450(cam) in the resting state-Investigations of enzyme models with pulse EPR and ENDOR spectroscopy
    • Aissaoui H, Bachmann R, Schweiger A, Woggon WD (1998) On the origin of the low-spin character of cytochrome P450(cam) in the resting state-Investigations of enzyme models with pulse EPR and ENDOR spectroscopy. Angew Chem Int Ed 37:2998-3002.
    • (1998) Angew Chem Int Ed , vol.37 , pp. 2998-3002
    • Aissaoui, H.1    Bachmann, R.2    Schweiger, A.3    Woggon, W.D.4
  • 45
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar SG (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15:5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 47
    • 12344259931 scopus 로고    scopus 로고
    • Dioxygen binding toasimplemyoglobin model in aqueous solution
    • KanoK, Kitagishi H, Kodera M, Hirota S (2005) Dioxygen binding toasimplemyoglobin model in aqueous solution. Angew Chem Int Ed 44:435-438.
    • (2005) Angew Chem Int Ed , vol.44 , pp. 435-438
    • Kano, K.1    Kitagishi, H.2    Kodera, M.3    Hirota, S.4
  • 48
  • 50
    • 0040268716 scopus 로고
    • A ferrous, high-spin heme-a model for cytochrome-a3 in the dioxygen reducing site of cytochrome-oxidase
    • Vansteelandtfrentrup J, Salmeen I, Babcock GT (1981) A ferrous, high-spin heme-a model for cytochrome-a3 in the dioxygen reducing site of cytochrome-oxidase. JAm Chem Soc 103:5981-5982.
    • (1981) JAm Chem Soc , vol.103 , pp. 5981-5982
    • Vansteelandtfrentrup, J.1    Salmeen, I.2    Babcock, G.T.3
  • 51
    • 0019883170 scopus 로고
    • Coordination geometries and vibrational properties of cytochromes-a and cytochromes-a3 in cytochrome-oxidase from soret excitation Raman spectroscopy
    • Babcock GT, Callahan PM, Ondrias MR, Salmeen I (1981)Coordination geometries and vibrational properties of cytochromes-a and cytochromes-a3 in cytochrome-oxidase from soret excitation Raman spectroscopy. Biochemistry20:959-966.
    • (1981) Biochemistry , vol.20 , pp. 959-966
    • Babcock, G.T.1    Callahan, P.M.2    Ondrias, M.R.3    Salmeen, I.4
  • 52
    • 34247195648 scopus 로고    scopus 로고
    • Syntheses of hemoprotein modelsthat can be covalently attached onto electrode surfaces by click chemistry
    • Decreau RA, Collman JP, Yang Y, Yan YL, Devaraj NK(2007) Syntheses of hemoprotein modelsthat can be covalently attached onto electrode surfaces by click chemistry. J Org Chem 72:2794-2802.
    • (2007) J Org Chem , vol.72 , pp. 2794-2802
    • Decreau, R.A.1    Collman, J.P.2    Yang, Y.3    Yan, Y.L.4    Devaraj, N.K.5


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