메뉴 건너뛰기




Volumn 108, Issue 34, 2011, Pages 14109-14114

Erratum: Adaptation of aerobic respiration to low O2 environments (Proceedings of the National Academy of Sciences of the United States of America (2011) 108, 34, (14109-14114) DOI: 10.1073/pnas.1018958108);Adaptation of aerobic respiration to low O2 environments

Author keywords

Cytochrome oxidase; Evolution

Indexed keywords

CYTOCHROME C OXIDASE; HEME COPPER OXIDOREDUCTASE; OXIDOREDUCTASE; OXYGEN; OXYGEN REDUCTASE; PROTON; PROTON PUMP; UNCLASSIFIED DRUG;

EID: 79960581689     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205903109     Document Type: Erratum
Times cited : (104)

References (42)
  • 1
    • 44449137093 scopus 로고    scopus 로고
    • The microbial engines that drive earth's biogeochemical cycles
    • DOI 10.1126/science.1153213
    • Falkowski PG, Fenchel T, Delong EF (2008) The microbial engines that drive Earth's biogeochemical cycles. Science 320:1034-1039. (Pubitemid 351929518)
    • (2008) Science , vol.320 , Issue.5879 , pp. 1034-1039
    • Falkowski, P.G.1    Fenchel, T.2    Delong, E.F.3
  • 2
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • DOI 10.1146/annurev.biochem.75.062003.101730
    • Hosler JP, Ferguson-Miller S, Mills DA (2006) Energy transduction: Proton transfer through the respiratory complexes. Annu Rev Biochem 75:165-187. (Pubitemid 44118030)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 3
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • DOI 10.1016/j.bbabio.2007.06.008, PII S0005272807001533
    • Wikstrom M, Verkhovsky MI (2007) Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases. Biochim Biophys Acta 1767:1200-1214. (Pubitemid 47498307)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1200-1214
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 5
    • 56449092797 scopus 로고    scopus 로고
    • The organization of proton motive and non-proton motive redox loops in prokaryotic respiratory systems
    • Simon J, van Spanning RJ, Richardson DJ (2008) The organization of proton motive and non-proton motive redox loops in prokaryotic respiratory systems. Biochim Biophys Acta 1777:1480-1490.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1480-1490
    • Simon, J.1    Van Spanning, R.J.2    Richardson, D.J.3
  • 6
    • 2542464946 scopus 로고    scopus 로고
    • Coupled proton and electron transfer reactions in cytochrome oxidase
    • Gennis RB (2004) Coupled proton and electron transfer reactions in cytochrome oxidase. Front Biosci 9:581-591.
    • (2004) Front Biosci , vol.9 , pp. 581-591
    • Gennis, R.B.1
  • 7
    • 44449146602 scopus 로고    scopus 로고
    • Diversity of the heme-copper superfamily in Archaea: Insights from genomics and structural modeling
    • Hemp J, Gennis RB (2008) Diversity of the heme-copper superfamily in Archaea: Insights from genomics and structural modeling. Results Probl Cell Differ 45:1-31.
    • (2008) Results Probl Cell Differ , vol.45 , pp. 1-31
    • Hemp, J.1    Gennis, R.B.2
  • 8
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • DOI 10.1016/S0005-2728(01)00169-4, PII S0005272801001694
    • Pereira MM, Santana M, TeixeiraM(2001) A novel scenario for the evolution of hemecopper oxygen reductases. Biochim Biophys Acta 1505:185-208. (Pubitemid 32378771)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.2-3 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 9
    • 33845989511 scopus 로고    scopus 로고
    • Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases
    • DOI 10.1021/bi062026u
    • Hemp J, et al. (2006) Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases. Biochemistry 45:15405-15410. (Pubitemid 46043109)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15405-15410
    • Hemp, J.1    Robinson, D.E.2    Ganesan, K.B.3    Martinez, T.J.4    Kelleher, N.L.5    Gennis, R.B.6
  • 10
    • 70349493006 scopus 로고    scopus 로고
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping. Proc Natl Acad Sci USA 106:16169-16173.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16169-16173
    • Chang, H.Y.1    Hemp, J.2    Chen, Y.3    Fee, J.A.4    Gennis, R.B.5
  • 11
    • 34548479264 scopus 로고    scopus 로고
    • 3 oxidase) of hemecopper oxygen reductases
    • 3 oxidase) of hemecopper oxygen reductases. Biochemistry 46:9963-9972.
    • (2007) Biochemistry , vol.46 , pp. 9963-9972
    • Hemp, J.1
  • 12
    • 0031688652 scopus 로고    scopus 로고
    • 3-type cytochrome c oxidase from Thermus thermophilus
    • 3-type cytochrome c oxidase from Thermus thermophilus. FEBS Lett 434:17-22.
    • (1998) FEBS Lett , vol.434 , pp. 17-22
    • Kannt, A.1
  • 13
    • 0034598409 scopus 로고    scopus 로고
    • Over-expression of cbaAB genes of Bacillus stearothermophilus produces a two-subunit SoxB-type cytochrome c oxidase with proton pumping activity
    • DOI 10.1016/S0005-2728(99)00102-4, PII S0005272899001024
    • Nikaido K, Sakamoto J, Noguchi S, Sone N (2000) Over-expression of cbaAB genes of Bacillus stearothermophilus produces a two-subunit SoxB-type cytochrome c oxidase with proton pumping activity. Biochim Biophys Acta 1456:35-44. (Pubitemid 30009736)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1456 , Issue.1 , pp. 35-44
    • Nikaido, K.1    Sakamoto, J.2    Noguchi, S.3    Sone, N.4
  • 18
    • 0017392734 scopus 로고
    • Purification and some properties of cytochrome c-552 from an extreme thermophile, Thermus thermophilus HB8
    • Hon-Nami K, Oshima T (1977) Purification and some properties of cytochrome c-552 from an extreme thermophile Thermus thermophilus HB8. J Biochem 82:769-776. (Pubitemid 8184272)
    • (1977) Journal of Biochemistry , vol.82 , Issue.3 , pp. 769-776
    • Hon-Nami, K.1    Oshima, T.2
  • 19
    • 77952739182 scopus 로고    scopus 로고
    • Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea
    • Walker CB, et al. (2010) Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea. Proc Natl Acad Sci USA 107:8818-8823.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8818-8823
    • Walker, C.B.1
  • 20
    • 39949085428 scopus 로고    scopus 로고
    • Electrostatic control of proton pumping in cytochrome c oxidase
    • Fadda E, Yu CH, Pomes R (2008) Electrostatic control of proton pumping in cytochrome c oxidase. Biochim Biophys Acta 1777:277-284.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 277-284
    • Fadda, E.1    Yu, C.H.2    Pomes, R.3
  • 22
    • 16344363592 scopus 로고    scopus 로고
    • Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck
    • DOI 10.1016/j.febslet.2005.02.051
    • Olsson MH, Sharma PK, Warshel A (2005) Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck. FEBS Lett 579:2026-2034. (Pubitemid 40469665)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2026-2034
    • Olsson, M.H.M.1    Sharma, P.K.2    Warshel, A.3
  • 23
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating
    • DOI 10.1016/j.febslet.2004.04.016, PII S0014579304004703
    • Popovic DM, Stuchebrukhov AA (2004) Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating. FEBS Lett 566:126-130. (Pubitemid 38625945)
    • (2004) FEBS Letters , vol.566 , Issue.1-3 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 24
    • 33748895869 scopus 로고    scopus 로고
    • Combined DFT and electrostatics study of the proton pumping mechanism in cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2005.12.003, PII S0005272805002793
    • Quenneville J, Popovic DM, Stuchebrukhov AA (2006) Combined DFTand electrostatics study of the proton pumping mechanism in cytochrome c oxidase. Biochim Biophys Acta 1757:1035-1046. (Pubitemid 44427750)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1035-1046
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 25
    • 57049130390 scopus 로고    scopus 로고
    • A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases
    • Sharpe MA, Ferguson-Miller S (2008) A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases. J Bioenerg Biomembr 40:541-549.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 541-549
    • Sharpe, M.A.1    Ferguson-Miller, S.2
  • 26
    • 58149147161 scopus 로고    scopus 로고
    • Proton pumping mechanism in cytochrome c oxidase
    • Siegbahn PE, Blomberg MR (2008) Proton pumping mechanism in cytochrome c oxidase. J Phys Chem A 112:12772-12780.
    • (2008) J Phys Chem A , vol.112 , pp. 12772-12780
    • Siegbahn, P.E.1    Blomberg, M.R.2
  • 28
    • 46349107814 scopus 로고    scopus 로고
    • Looking for the minimum common denominator in heme-copper oxygen reductases: Towards a unified catalytic mechanism
    • Pereira MM, Sousa FL, Verissimo AF, Teixeira M (2008) Looking for the minimum common denominator in heme-copper oxygen reductases: Towards a unified catalytic mechanism. Biochim Biophys Acta 1777:929-934.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 929-934
    • Pereira, M.M.1    Sousa, F.L.2    Verissimo, A.F.3    Teixeira, M.4
  • 30
    • 78249242740 scopus 로고    scopus 로고
    • The identity of the transient proton loading site of the proton-pumping mechanism of cytochrome c oxidase
    • Kaila VR, Sharma V, Wikstrom M (2011) The identity of the transient proton loading site of the proton-pumping mechanism of cytochrome c oxidase. Biochim Biophys Acta 1807:80-84.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 80-84
    • Kaila, V.R.1    Sharma, V.2    Wikstrom, M.3
  • 31
    • 77954809358 scopus 로고    scopus 로고
    • 3 cytochrome oxidase provides insights into proton pumping
    • 3 cytochrome oxidase provides insights into proton pumping. Science 329:327-330.
    • (2010) Science , vol.329 , pp. 327-330
    • Buschmann, S.1
  • 32
    • 36549060589 scopus 로고    scopus 로고
    • 3 oxidase from Thermus thermophilus
    • 3 oxidase from Thermus thermophilus. Biochim Biophys Acta 1767:1383-1392.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1383-1392
    • Siletsky, S.A.1
  • 37
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M, et al. (2002) The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J Mol Biol 321:329-339.
    • (2002) J Mol Biol , vol.321 , pp. 329-339
    • Svensson-Ek, M.1
  • 38
    • 42349083650 scopus 로고    scopus 로고
    • 3from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases
    • 3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases. Biochemistry 47:4657-4665.
    • (2008) Biochemistry , vol.47 , pp. 4657-4665
    • Luna, V.M.1    Chen, Y.2    Fee, J.A.3    Stout, C.D.4
  • 39
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • Verkhovsky MI, Morgan JE, Wikstrom M (1994) Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase. Biochemistry 33:3079-3086. (Pubitemid 24103371)
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikstrom, M.3
  • 40
    • 57449106295 scopus 로고    scopus 로고
    • Identification of components of electron transport chains in the extremely thermoacidophilic crenarchaeon Metallosphaera sedula through iron and sulfur compound oxidation transcriptomes
    • Auernik KS, Kelly RM (2008) Identification of components of electron transport chains in the extremely thermoacidophilic crenarchaeon Metallosphaera sedula through iron and sulfur compound oxidation transcriptomes. Appl EnvironMicrobiol 74:7723-7732.
    • (2008) Appl EnvironMicrobiol , vol.74 , pp. 7723-7732
    • Auernik, K.S.1    Kelly, R.M.2
  • 42
    • 77957937698 scopus 로고    scopus 로고
    • Iron-oxidizing bacteria: An environmental and genomic perspective
    • Emerson D, Fleming EJ, McBeth JM (2010) Iron-oxidizing bacteria: An environmental and genomic perspective. Annu Rev Microbiol 64:561-583.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 561-583
    • Emerson, D.1    Fleming, E.J.2    McBeth, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.